C7150 Regulation of metabolism
Faculty of ScienceAutumn 2024
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
In-person direct teaching - Teacher(s)
- prof. Mgr. Tomáš Kašparovský, Ph.D. (lecturer)
Mgr. Gabriela Ilčíková (assistant)
RNDr. Jitka Kašparovská, Ph.D. (assistant) - Guaranteed by
- prof. Mgr. Tomáš Kašparovský, Ph.D.
Department of Biochemistry – Chemistry Section – Faculty of Science
Supplier department: Department of Biochemistry – Chemistry Section – Faculty of Science - Timetable
- Mon 9:00–10:50 B11/335
- Prerequisites
- C4182 Biochemistry II || C3580 Biochemistry || C5720 Biochemistry || LF:BLBC0211p Biochemistry - lecture
Elementary biochemistry - Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 21 fields of study the course is directly associated with, display
- Course objectives
- Control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
- Learning outcomes
- At the end of the course, students should be able to: - describe and explain the main metabolic pathways in bacteria and eukaryots; - analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism; - reproduce and present their extended knowledge of dynamic biochemistry and enzymology; - demonstrate new information on biomedical aspects of biochemistry.
- Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- SILBERNAGL, Stefan and Agamemnon DESPOPOULOS. Atlas fyziologie člověka : 201 barevných tabulí. Translated by Otomar Kittnar. 4. české vydání. Praha: Grada Publishing, 2016, xv, 434. ISBN 9788024742717. info
- KRAUSS, Gerhard. Biochemistry of signal transduction and regulation. 5th, completely rev. ed. Weinheim: Wiley-VCH, 2014, xxviii, 81. ISBN 9783527333660. info
- KOOLMAN, Jan and Klaus-Heinrich RÖHM. Barevný atlas biochemie. Translated by Vladimír Benda - Martin Vejražka - Jiří Jonák. 1. české vydání. Praha: Grada, 2012, xiv, 498. ISBN 9788024729770. info
- KITTNAR, Otomar and Mikuláš MLČEK. Atlas fyziologických regulací. 1. vyd. Praha: Grada, 2009, 316 s. ISBN 9788024727226. info
- HOLEČEK, Milan. Regulace metabolizmu cukrů, tuků, bílkovin a aminokyselin. 1. vyd. Praha: Grada, 2006, 286 s. ISBN 8024715627. info
- Teaching methods
- Series of lectures
- Assessment methods
- Writing examination. According to epidemiological measures, either on-site or remotely.
- Language of instruction
- Czech
- Further Comments
- The course is taught annually.
C7150 Regulation of metabolism
Faculty of ScienceAutumn 2023
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
- Teacher(s)
- prof. Mgr. Tomáš Kašparovský, Ph.D. (lecturer)
Mgr. Gabriela Ilčíková (assistant)
RNDr. Jitka Kašparovská, Ph.D. (assistant) - Guaranteed by
- prof. Mgr. Tomáš Kašparovský, Ph.D.
Department of Biochemistry – Chemistry Section – Faculty of Science
Supplier department: Department of Biochemistry – Chemistry Section – Faculty of Science - Timetable
- Mon 9:00–10:50 B11/335
- Prerequisites
- C4182 Biochemistry II || C3580 Biochemistry || C5720 Biochemistry || LF:BLBC0211p Biochemistry - lecture
Elementary biochemistry - Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 21 fields of study the course is directly associated with, display
- Course objectives
- Control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
- Learning outcomes
- At the end of the course, students should be able to: - describe and explain the main metabolic pathways in bacteria and eukaryots; - analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism; - reproduce and present their extended knowledge of dynamic biochemistry and enzymology; - demonstrate new information on biomedical aspects of biochemistry.
- Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- SILBERNAGL, Stefan and Agamemnon DESPOPOULOS. Atlas fyziologie člověka : 201 barevných tabulí. Translated by Otomar Kittnar. 4. české vydání. Praha: Grada Publishing, 2016, xv, 434. ISBN 9788024742717. info
- KRAUSS, Gerhard. Biochemistry of signal transduction and regulation. 5th, completely rev. ed. Weinheim: Wiley-VCH, 2014, xxviii, 81. ISBN 9783527333660. info
- KOOLMAN, Jan and Klaus-Heinrich RÖHM. Barevný atlas biochemie. Translated by Vladimír Benda - Martin Vejražka - Jiří Jonák. 1. české vydání. Praha: Grada, 2012, xiv, 498. ISBN 9788024729770. info
- KITTNAR, Otomar and Mikuláš MLČEK. Atlas fyziologických regulací. 1. vyd. Praha: Grada, 2009, 316 s. ISBN 9788024727226. info
- HOLEČEK, Milan. Regulace metabolizmu cukrů, tuků, bílkovin a aminokyselin. 1. vyd. Praha: Grada, 2006, 286 s. ISBN 8024715627. info
- Teaching methods
- Series of lectures
- Assessment methods
- Writing examination. According to epidemiological measures, either on-site or remotely.
- Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually.
C7150 Regulation of metabolism
Faculty of ScienceAutumn 2022
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
- Teacher(s)
- prof. Mgr. Tomáš Kašparovský, Ph.D. (lecturer)
Mgr. Gabriela Ilčíková (assistant)
RNDr. Jitka Kašparovská, Ph.D. (assistant) - Guaranteed by
- prof. Mgr. Tomáš Kašparovský, Ph.D.
Department of Biochemistry – Chemistry Section – Faculty of Science
Supplier department: Department of Biochemistry – Chemistry Section – Faculty of Science - Timetable
- Mon 9:00–10:50 B11/335
- Prerequisites
- C4182 Biochemistry II || C3580 Biochemistry || C5720 Biochemistry || LF:BLBC0211p Biochemistry - lecture
Elementary biochemistry - Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 23 fields of study the course is directly associated with, display
- Course objectives
- Control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
- Learning outcomes
- At the end of the course, students should be able to: - describe and explain the main metabolic pathways in bacteria and eukaryots; - analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism; - reproduce and present their extended knowledge of dynamic biochemistry and enzymology; - demonstrate new information on biomedical aspects of biochemistry.
- Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- SILBERNAGL, Stefan and Agamemnon DESPOPOULOS. Atlas fyziologie člověka : 201 barevných tabulí. Translated by Otomar Kittnar. 4. české vydání. Praha: Grada Publishing, 2016, xv, 434. ISBN 9788024742717. info
- KRAUSS, Gerhard. Biochemistry of signal transduction and regulation. 5th, completely rev. ed. Weinheim: Wiley-VCH, 2014, xxviii, 81. ISBN 9783527333660. info
- KOOLMAN, Jan and Klaus-Heinrich RÖHM. Barevný atlas biochemie. Translated by Vladimír Benda - Martin Vejražka - Jiří Jonák. 1. české vydání. Praha: Grada, 2012, xiv, 498. ISBN 9788024729770. info
- KITTNAR, Otomar and Mikuláš MLČEK. Atlas fyziologických regulací. 1. vyd. Praha: Grada, 2009, 316 s. ISBN 9788024727226. info
- HOLEČEK, Milan. Regulace metabolizmu cukrů, tuků, bílkovin a aminokyselin. 1. vyd. Praha: Grada, 2006, 286 s. ISBN 8024715627. info
- Teaching methods
- Series of lectures
- Assessment methods
- Writing examination. According to epidemiological measures, either on-site or remotely.
- Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually.
C7150 Regulation of metabolism
Faculty of Scienceautumn 2021
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
- Teacher(s)
- prof. Mgr. Tomáš Kašparovský, Ph.D. (lecturer)
RNDr. Jitka Kašparovská, Ph.D. (assistant)
Mgr. et Mgr. Natálie Nádeníčková (assistant) - Guaranteed by
- prof. Mgr. Tomáš Kašparovský, Ph.D.
Department of Biochemistry – Chemistry Section – Faculty of Science
Supplier department: Department of Biochemistry – Chemistry Section – Faculty of Science - Timetable
- Mon 9:00–10:50 B11/335
- Prerequisites
- C4182 Biochemistry II || C3580 Biochemistry || C5720 Biochemistry
Elementary biochemistry - Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 23 fields of study the course is directly associated with, display
- Course objectives
- Control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
- Learning outcomes
- At the end of the course, students should be able to: - describe and explain the main metabolic pathways in bacteria and eukaryots; - analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism; - reproduce and present their extended knowledge of dynamic biochemistry and enzymology; - demonstrate new information on biomedical aspects of biochemistry.
- Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- SILBERNAGL, Stefan and Agamemnon DESPOPOULOS. Atlas fyziologie člověka : 201 barevných tabulí. Translated by Otomar Kittnar. 4. české vydání. Praha: Grada Publishing, 2016, xv, 434. ISBN 9788024742717. info
- KRAUSS, Gerhard. Biochemistry of signal transduction and regulation. 5th, completely rev. ed. Weinheim: Wiley-VCH, 2014, xxviii, 81. ISBN 9783527333660. info
- KOOLMAN, Jan and Klaus-Heinrich RÖHM. Barevný atlas biochemie. Translated by Vladimír Benda - Martin Vejražka - Jiří Jonák. 1. české vydání. Praha: Grada, 2012, xiv, 498. ISBN 9788024729770. info
- KITTNAR, Otomar and Mikuláš MLČEK. Atlas fyziologických regulací. 1. vyd. Praha: Grada, 2009, 316 s. ISBN 9788024727226. info
- HOLEČEK, Milan. Regulace metabolizmu cukrů, tuků, bílkovin a aminokyselin. 1. vyd. Praha: Grada, 2006, 286 s. ISBN 8024715627. info
- Teaching methods
- Series of lectures
- Assessment methods
- Writing examination. According to epidemiological measures, either on-site or remotely.
- Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually.
C7150 Regulation of metabolism
Faculty of ScienceAutumn 2020
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
- Teacher(s)
- prof. Mgr. Tomáš Kašparovský, Ph.D. (lecturer)
RNDr. Jitka Kašparovská, Ph.D. (assistant)
Mgr. et Mgr. Natálie Nádeníčková (assistant) - Guaranteed by
- prof. Mgr. Tomáš Kašparovský, Ph.D.
Department of Biochemistry – Chemistry Section – Faculty of Science
Supplier department: Department of Biochemistry – Chemistry Section – Faculty of Science - Timetable
- Mon 9:00–10:50 prace doma
- Prerequisites
- C4182 Biochemistry II || C3580 Biochemistry || C5720 Biochemistry
Elementary biochemistry - Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 23 fields of study the course is directly associated with, display
- Course objectives
- Control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
- Learning outcomes
- At the end of the course, students should be able to: - describe and explain the main metabolic pathways in bacteria and eukaryots; - analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism; - reproduce and present their extended knowledge of dynamic biochemistry and enzymology; - demonstrate new information on biomedical aspects of biochemistry.
- Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- SILBERNAGL, Stefan and Agamemnon DESPOPOULOS. Atlas fyziologie člověka : 201 barevných tabulí. Translated by Otomar Kittnar. 4. české vydání. Praha: Grada Publishing, 2016, xv, 434. ISBN 9788024742717. info
- KRAUSS, Gerhard. Biochemistry of signal transduction and regulation. 5th, completely rev. ed. Weinheim: Wiley-VCH, 2014, xxviii, 81. ISBN 9783527333660. info
- KOOLMAN, Jan and Klaus-Heinrich RÖHM. Barevný atlas biochemie. Translated by Vladimír Benda - Martin Vejražka - Jiří Jonák. 1. české vydání. Praha: Grada, 2012, xiv, 498. ISBN 9788024729770. info
- KITTNAR, Otomar and Mikuláš MLČEK. Atlas fyziologických regulací. 1. vyd. Praha: Grada, 2009, 316 s. ISBN 9788024727226. info
- HOLEČEK, Milan. Regulace metabolizmu cukrů, tuků, bílkovin a aminokyselin. 1. vyd. Praha: Grada, 2006, 286 s. ISBN 8024715627. info
- Teaching methods
- Series of lectures
- Assessment methods
- Writing examination. According to epidemiological measures, either on-site or remotely.
- Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually.
C7150 Regulation of metabolism
Faculty of ScienceAutumn 2019
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
- Teacher(s)
- prof. Mgr. Tomáš Kašparovský, Ph.D. (lecturer)
RNDr. Jitka Kašparovská, Ph.D. (assistant)
Mgr. et Mgr. Natálie Nádeníčková (assistant) - Guaranteed by
- prof. Mgr. Tomáš Kašparovský, Ph.D.
Department of Biochemistry – Chemistry Section – Faculty of Science
Supplier department: Department of Biochemistry – Chemistry Section – Faculty of Science - Timetable
- Mon 9:00–10:50 B11/335
- Prerequisites
- C4182 Biochemistry II || C3580 Biochemistry || C5720 Biochemistry
Elementary biochemistry - Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 23 fields of study the course is directly associated with, display
- Course objectives
- Control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
- Learning outcomes
- At the end of the course, students should be able to: - describe and explain the main metabolic pathways in bacteria and eukaryots; - analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism; - reproduce and present their extended knowledge of dynamic biochemistry and enzymology; - demonstrate new information on biomedical aspects of biochemistry.
- Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- SILBERNAGL, Stefan and Agamemnon DESPOPOULOS. Atlas fyziologie člověka : 201 barevných tabulí. Translated by Otomar Kittnar. 4. české vydání. Praha: Grada Publishing, 2016, xv, 434. ISBN 9788024742717. info
- KRAUSS, Gerhard. Biochemistry of signal transduction and regulation. 5th, completely rev. ed. Weinheim: Wiley-VCH, 2014, xxviii, 81. ISBN 9783527333660. info
- KOOLMAN, Jan and Klaus-Heinrich RÖHM. Barevný atlas biochemie. Translated by Vladimír Benda - Martin Vejražka - Jiří Jonák. 1. české vydání. Praha: Grada, 2012, xiv, 498. ISBN 9788024729770. info
- KITTNAR, Otomar and Mikuláš MLČEK. Atlas fyziologických regulací. 1. vyd. Praha: Grada, 2009, 316 s. ISBN 9788024727226. info
- HOLEČEK, Milan. Regulace metabolizmu cukrů, tuků, bílkovin a aminokyselin. 1. vyd. Praha: Grada, 2006, 286 s. ISBN 8024715627. info
- Teaching methods
- Series of lectures
- Assessment methods
- Writing examination.
- Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually.
C7150 Regulation of metabolism
Faculty of ScienceAutumn 2018
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
- Teacher(s)
- prof. Mgr. Tomáš Kašparovský, Ph.D. (lecturer)
RNDr. Jitka Kašparovská, Ph.D. (assistant) - Guaranteed by
- prof. Mgr. Tomáš Kašparovský, Ph.D.
Department of Biochemistry – Chemistry Section – Faculty of Science
Supplier department: Department of Biochemistry – Chemistry Section – Faculty of Science - Timetable
- Mon 17. 9. to Sun 30. 9. Mon 9:00–10:50 B17/432, Mon 1. 10. to Fri 14. 12. Mon 9:00–10:50 B11/335
- Prerequisites (in Czech)
- C4182 Biochemistry II || C3580 Biochemistry || C5720 Biochemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 23 fields of study the course is directly associated with, display
- Course objectives
- Dynamic biochemistry I - control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
Learning outcomes:
At the end of the course, students should be able to:
- describe and explain the main metabolic pathways in bacteria and eukaryots;
- analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism;
- reproduce and present their extended knowledge of dynamic biochemistry and enzymology;
- demonstrate new information on biomedical aspects of biochemistry. - Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- SILBERNAGL, Stefan and Agamemnon DESPOPOULOS. Atlas fyziologie člověka : 201 barevných tabulí. Translated by Otomar Kittnar. 4. české vydání. Praha: Grada Publishing, 2016, xv, 434. ISBN 9788024742717. info
- KRAUSS, Gerhard. Biochemistry of signal transduction and regulation. 5th, completely rev. ed. Weinheim: Wiley-VCH, 2014, xxviii, 81. ISBN 9783527333660. info
- KOOLMAN, Jan and Klaus-Heinrich RÖHM. Barevný atlas biochemie. Translated by Vladimír Benda - Martin Vejražka - Jiří Jonák. 1. české vydání. Praha: Grada, 2012, xiv, 498. ISBN 9788024729770. info
- KITTNAR, Otomar and Mikuláš MLČEK. Atlas fyziologických regulací. 1. vyd. Praha: Grada, 2009, 316 s. ISBN 9788024727226. info
- HOLEČEK, Milan. Regulace metabolizmu cukrů, tuků, bílkovin a aminokyselin. 1. vyd. Praha: Grada, 2006, 286 s. ISBN 8024715627. info
- Teaching methods
- Series of lectures
- Assessment methods
- Writing examination.
- Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually.
C7150 Regulation of metabolism
Faculty of Scienceautumn 2017
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
- Teacher(s)
- prof. Mgr. Tomáš Kašparovský, Ph.D. (lecturer)
RNDr. Jitka Kašparovská, Ph.D. (assistant) - Guaranteed by
- prof. RNDr. Zdeněk Glatz, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Supplier department: Department of Biochemistry – Chemistry Section – Faculty of Science - Timetable
- Mon 18. 9. to Fri 15. 12. Fri 10:00–11:50 B11/205
- Prerequisites (in Czech)
- C4182 Biochemistry II || C3580 Biochemistry || C5720 Biochemistry
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 23 fields of study the course is directly associated with, display
- Course objectives
- Dynamic biochemistry I - control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
Learning outcomes:
At the end of the course, students should be able to:
- describe and explain the main metabolic pathways in bacteria and eukaryots;
- analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism;
- reproduce and present their extended knowledge of dynamic biochemistry and enzymology;
- demonstrate new information on biomedical aspects of biochemistry. - Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- SILBERNAGL, Stefan and Agamemnon DESPOPOULOS. Atlas fyziologie člověka : 201 barevných tabulí. Translated by Otomar Kittnar. 4. české vydání. Praha: Grada Publishing, 2016, xv, 434. ISBN 9788024742717. info
- KRAUSS, Gerhard. Biochemistry of signal transduction and regulation. 5th, completely rev. ed. Weinheim: Wiley-VCH, 2014, xxviii, 81. ISBN 9783527333660. info
- KOOLMAN, Jan and Klaus-Heinrich RÖHM. Barevný atlas biochemie. Translated by Vladimír Benda - Martin Vejražka - Jiří Jonák. 1. české vydání. Praha: Grada, 2012, xiv, 498. ISBN 9788024729770. info
- KITTNAR, Otomar and Mikuláš MLČEK. Atlas fyziologických regulací. 1. vyd. Praha: Grada, 2009, 316 s. ISBN 9788024727226. info
- HOLEČEK, Milan. Regulace metabolizmu cukrů, tuků, bílkovin a aminokyselin. 1. vyd. Praha: Grada, 2006, 286 s. ISBN 8024715627. info
- Teaching methods
- Series of lectures
- Assessment methods
- Writing examination.
- Language of instruction
- Czech
- Further Comments
- Study Materials
The course is taught annually.
C7150 Dynamic biochemistry I - control of metabolism
Faculty of ScienceAutumn 2016
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc.
Supplier department: Department of Biochemistry – Chemistry Section – Faculty of Science - Timetable
- Mon 19. 9. to Sun 18. 12. Mon 13:00–14:50 C05/107
- Prerequisites
- Could be registered in the 3rd, 5th, 7th, 9th semester
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 23 fields of study the course is directly associated with, display
- Course objectives
- Dynamic biochemistry I - control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
Learning outcomes:
At the end of the course, students should be able to:
- describe and explain the main metabolic pathways in bacteria and eukaryots;
- analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism;
- reproduce and present their extended knowledge of dynamic biochemistry and enzymology;
- demonstrate new information on biomedical aspects of biochemistry. - Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- STOREY, K.B. (ed.). Functional Metabolism: Regulation and Adaptation. Hoboken, New Jersey: Wiley-Liss, Inc., 2004, 594 pp. ISBN 0-471-41090-X. info
- Biochemistry. Edited by Donald Voet - Judith G. Voet. 3rd ed. Hoboken, N.J.: John Wiley & Sons, 2004, xv, 1591 s. ISBN 0-471-41761-0. info
- BERG, J.M., J.L. TYMOCZKO and L. STRYER. Biochemistry. 5th. New York: W.H. Freeman and Company, 2002, 974 pp. ISBN 0-7167-4684-0. info
- NELSON, D.L. and M.M. COX. Lehninger Principles of Biochemistry. 3rd. New York: Worth Publishers, 2000, 1152 pp. ISBN 1-57259-153-6. info
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Compensatory contents: Ca. 200 slides/foils available at the lecturer
- Teaching methods
- Series of lectures
- Assessment methods
- Lectures, abundantly documented with charts, diagrams, formulas and figures, which are offered to the students for making copies. Oral examination; 40 specified questions are at disposal.
- Language of instruction
- Czech
- Follow-Up Courses
- Further comments (probably available only in Czech)
- Study Materials
The course is taught annually.
Information on course enrolment limitations: Při týdenní výuce min. 8 posluchačů, při blokové bez omezení
C7150 Dynamic biochemistry I - control of metabolism
Faculty of ScienceAutumn 2015
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc.
Supplier department: Department of Biochemistry – Chemistry Section – Faculty of Science - Timetable
- Thu 14:00–15:50 C05/114
- Prerequisites
- Could be registered in the 3rd, 5th, 7th, 9th semester
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 23 fields of study the course is directly associated with, display
- Course objectives
- Dynamic biochemistry I - control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
Learning outcomes:
At the end of the course, students should be able to:
- describe and explain the main metabolic pathways in bacteria and eukaryots;
- analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism;
- reproduce and present their extended knowledge of dynamic biochemistry and enzymology;
- demonstrate new information on biomedical aspects of biochemistry. - Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- STOREY, K.B. (ed.). Functional Metabolism: Regulation and Adaptation. Hoboken, New Jersey: Wiley-Liss, Inc., 2004, 594 pp. ISBN 0-471-41090-X. info
- Biochemistry. Edited by Donald Voet - Judith G. Voet. 3rd ed. Hoboken, N.J.: John Wiley & Sons, 2004, xv, 1591 s. ISBN 0-471-41761-0. info
- BERG, J.M., J.L. TYMOCZKO and L. STRYER. Biochemistry. 5th. New York: W.H. Freeman and Company, 2002, 974 pp. ISBN 0-7167-4684-0. info
- NELSON, D.L. and M.M. COX. Lehninger Principles of Biochemistry. 3rd. New York: Worth Publishers, 2000, 1152 pp. ISBN 1-57259-153-6. info
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Compensatory contents: Ca. 200 slides/foils available at the lecturer
- Teaching methods
- Series of lectures
- Assessment methods
- Lectures, abundantly documented with charts, diagrams, formulas and figures, which are offered to the students for making copies. Oral examination; 40 specified questions are at disposal.
- Language of instruction
- Czech
- Follow-Up Courses
- Further comments (probably available only in Czech)
- The course is taught annually.
Information on course enrolment limitations: Při týdenní výuce min. 8 posluchačů, při blokové bez omezení
C7150 Dynamic biochemistry I - control of metabolism
Faculty of ScienceAutumn 2014
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc.
Supplier department: Department of Biochemistry – Chemistry Section – Faculty of Science - Timetable
- Fri 10:00–11:50 C05/114
- Prerequisites
- Could be registered in the 3rd, 5th, 7th, 9th semester
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 23 fields of study the course is directly associated with, display
- Course objectives
- Dynamic biochemistry I - control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
Learning outcomes:
At the end of the course, students should be able to:
- describe and explain the main metabolic pathways in bacteria and eukaryots;
- analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism;
- reproduce and present their extended knowledge of dynamic biochemistry and enzymology;
- demonstrate new information on biomedical aspects of biochemistry. - Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- STOREY, K.B. (ed.). Functional Metabolism: Regulation and Adaptation. Hoboken, New Jersey: Wiley-Liss, Inc., 2004, 594 pp. ISBN 0-471-41090-X. info
- Biochemistry. Edited by Donald Voet - Judith G. Voet. 3rd ed. Hoboken, N.J.: John Wiley & Sons, 2004, xv, 1591 s. ISBN 0-471-41761-0. info
- BERG, J.M., J.L. TYMOCZKO and L. STRYER. Biochemistry. 5th. New York: W.H. Freeman and Company, 2002, 974 pp. ISBN 0-7167-4684-0. info
- NELSON, D.L. and M.M. COX. Lehninger Principles of Biochemistry. 3rd. New York: Worth Publishers, 2000, 1152 pp. ISBN 1-57259-153-6. info
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Compensatory contents: Ca. 200 slides/foils available at the lecturer
- Teaching methods
- Series of lectures
- Assessment methods
- Lectures, abundantly documented with charts, diagrams, formulas and figures, which are offered to the students for making copies. Oral examination; 40 specified questions are at disposal.
- Language of instruction
- Czech
- Follow-Up Courses
- Further comments (probably available only in Czech)
- Study Materials
The course is taught annually.
Information on course enrolment limitations: Při týdenní výuce min. 8 posluchačů, při blokové bez omezení
C7150 Dynamic biochemistry I - control of metabolism
Faculty of ScienceAutumn 2013
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc.
Supplier department: Department of Biochemistry – Chemistry Section – Faculty of Science - Timetable
- Fri 8:00–9:50 B11/205
- Prerequisites
- Could be registered in the 3rd, 5th, 7th, 9th semester
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 23 fields of study the course is directly associated with, display
- Course objectives
- Dynamic biochemistry I - control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
Learning outcomes:
At the end of the course, students should be able to:
- describe and explain the main metabolic pathways in bacteria and eukaryots;
- analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism;
- reproduce and present their extended knowledge of dynamic biochemistry and enzymology;
- demonstrate new information on biomedical aspects of biochemistry. - Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- STOREY, K.B. (ed.). Functional Metabolism: Regulation and Adaptation. Hoboken, New Jersey: Wiley-Liss, Inc., 2004, 594 pp. ISBN 0-471-41090-X. info
- Biochemistry. Edited by Donald Voet - Judith G. Voet. 3rd ed. Hoboken, N.J.: John Wiley & Sons, 2004, xv, 1591 s. ISBN 0-471-41761-0. info
- BERG, J.M., J.L. TYMOCZKO and L. STRYER. Biochemistry. 5th. New York: W.H. Freeman and Company, 2002, 974 pp. ISBN 0-7167-4684-0. info
- NELSON, D.L. and M.M. COX. Lehninger Principles of Biochemistry. 3rd. New York: Worth Publishers, 2000, 1152 pp. ISBN 1-57259-153-6. info
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Compensatory contents: Ca. 200 slides/foils available at the lecturer
- Teaching methods
- Series of lectures
- Assessment methods
- Lectures, abundantly documented with charts, diagrams, formulas and figures, which are offered to the students for making copies. Oral examination; 40 specified questions are at disposal.
- Language of instruction
- Czech
- Follow-Up Courses
- Further comments (probably available only in Czech)
- The course is taught annually.
Information on course enrolment limitations: Při týdenní výuce min. 8 posluchačů, při blokové bez omezení
C7150 Dynamic biochemistry I - control of metabolism
Faculty of ScienceAutumn 2012
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc.
Supplier department: Department of Biochemistry – Chemistry Section – Faculty of Science - Timetable
- Tue 11:00–12:50 C05/114
- Prerequisites
- Could be registered in the 3rd, 5th, 7th, 9th semester
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 23 fields of study the course is directly associated with, display
- Course objectives
- Dynamic biochemistry I - control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
Learning outcomes:
At the end of the course, students should be able to:
- describe and explain the main metabolic pathways in bacteria and eukaryots;
- analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism;
- reproduce and present their extended knowledge of dynamic biochemistry and enzymology;
- demonstrate new information on biomedical aspects of biochemistry. - Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- STOREY, K.B. (ed.). Functional Metabolism: Regulation and Adaptation. Hoboken, New Jersey: Wiley-Liss, Inc., 2004, 594 pp. ISBN 0-471-41090-X. info
- Biochemistry. Edited by Donald Voet - Judith G. Voet. 3rd ed. Hoboken, N.J.: John Wiley & Sons, 2004, xv, 1591 s. ISBN 0-471-41761-0. info
- BERG, J.M., J.L. TYMOCZKO and L. STRYER. Biochemistry. 5th. New York: W.H. Freeman and Company, 2002, 974 pp. ISBN 0-7167-4684-0. info
- NELSON, D.L. and M.M. COX. Lehninger Principles of Biochemistry. 3rd. New York: Worth Publishers, 2000, 1152 pp. ISBN 1-57259-153-6. info
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Teaching methods
- Series of lectures
- Assessment methods
- Lectures, abundantly documented with charts, diagrams, formulas and figures, which are offered to the students for making copies. Oral examination; 40 specified questions are at disposal.
- Language of instruction
- Czech
- Follow-Up Courses
- Further comments (probably available only in Czech)
- Study Materials
The course is taught annually.
Information on course enrolment limitations: Při týdenní výuce min. 8 posluchačů, při blokové bez omezení
C7150 Dynamic biochemistry I - control of metabolism
Faculty of ScienceAutumn 2011
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc. - Timetable
- Tue 9:00–10:50 C05/114
- Prerequisites
- Could be registered in the 3rd, 5th, 7th, 9th semester
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 23 fields of study the course is directly associated with, display
- Course objectives
- Dynamic biochemistry I - control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
Learning outcomes:
At the end of the course, students should be able to:
- describe and explain the main metabolic pathways in bacteria and eukaryots;
- analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism;
- reproduce and present their extended knowledge of dynamic biochemistry and enzymology;
- demonstrate new information on biomedical aspects of biochemistry. - Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- STOREY, K.B. (ed.). Functional Metabolism: Regulation and Adaptation. Hoboken, New Jersey: Wiley-Liss, Inc., 2004, 594 pp. ISBN 0-471-41090-X. info
- Biochemistry. Edited by Donald Voet - Judith G. Voet. 3rd ed. Hoboken, N.J.: John Wiley & Sons, 2004, xv, 1591 s. ISBN 0-471-41761-0. info
- BERG, J.M., J.L. TYMOCZKO and L. STRYER. Biochemistry. 5th. New York: W.H. Freeman and Company, 2002, 974 pp. ISBN 0-7167-4684-0. info
- NELSON, D.L. and M.M. COX. Lehninger Principles of Biochemistry. 3rd. New York: Worth Publishers, 2000, 1152 pp. ISBN 1-57259-153-6. info
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Teaching methods
- Series of lectures
- Assessment methods
- Lectures, abundantly documented with charts, diagrams, formulas and figures, which are offered to the students for making copies. Oral examination; 40 specified questions are at disposal.
- Language of instruction
- Czech
- Follow-Up Courses
- Further comments (probably available only in Czech)
- Study Materials
The course is taught annually.
Information on course enrolment limitations: Při týdenní výuce min. 8 posluchačů, při blokové bez omezení
C7150 Dynamic biochemistry I - control of metabolism
Faculty of ScienceAutumn 2010
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc. - Timetable
- Wed 12:00–13:50 C05/114
- Prerequisites
- Could be registered in the 3rd, 5th, 7th, 9th semester
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 20 fields of study the course is directly associated with, display
- Course objectives
- Dynamic biochemistry I - control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
Learning outcomes:
At the end of the course, students should be able to:
- describe and explain the main metabolic pathways in bacteria and eukaryots;
- analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism;
- reproduce and present their extended knowledge of dynamic biochemistry and enzymology;
- demonstrate new information on biomedical aspects of biochemistry. - Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- STOREY, K.B. (ed.). Functional Metabolism: Regulation and Adaptation. Hoboken, New Jersey: Wiley-Liss, Inc., 2004, 594 pp. ISBN 0-471-41090-X. info
- Biochemistry. Edited by Donald Voet - Judith G. Voet. 3rd ed. Hoboken, N.J.: John Wiley & Sons, 2004, xv, 1591 s. ISBN 0-471-41761-0. info
- BERG, J.M., J.L. TYMOCZKO and L. STRYER. Biochemistry. 5th. New York: W.H. Freeman and Company, 2002, 974 pp. ISBN 0-7167-4684-0. info
- NELSON, D.L. and M.M. COX. Lehninger Principles of Biochemistry. 3rd. New York: Worth Publishers, 2000, 1152 pp. ISBN 1-57259-153-6. info
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Teaching methods
- Series of lectures
- Assessment methods
- Lectures, abundantly documented with charts, diagrams, formulas and figures, which are offered to the students for making copies. Oral examination; 40 specified questions are at disposal.
- Language of instruction
- Czech
- Follow-Up Courses
- Further comments (probably available only in Czech)
- Study Materials
The course is taught annually.
Information on course enrolment limitations: Při týdenní výuce min. 8 posluchačů, při blokové bez omezení
C7150 Dynamic biochemistry I - control of metabolism
Faculty of ScienceAutumn 2009
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc. - Timetable
- Tue 18:00–19:50 C05/114
- Prerequisites
- Could be registered in the 3rd, 5th, 7th, 9th semester
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 20 fields of study the course is directly associated with, display
- Course objectives
- Dynamic biochemistry I - control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
Learning outcomes:
At the end of the course, students should be able to:
- describe and explain the main metabolic pathways in bacteria and eukaryots;
- analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism;
- reproduce and present their extended knowledge of dynamic biochemistry and enzymology;
- demonstrate new information on biomedical aspects of biochemistry. - Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- STOREY, K.B. (ed.). Functional Metabolism: Regulation and Adaptation. Hoboken, New Jersey: Wiley-Liss, Inc., 2004, 594 pp. ISBN 0-471-41090-X. info
- Biochemistry. Edited by Donald Voet - Judith G. Voet. 3rd ed. Hoboken, N.J.: John Wiley & Sons, 2004, xv, 1591 s. ISBN 0-471-41761-0. info
- BERG, J.M., J.L. TYMOCZKO and L. STRYER. Biochemistry. 5th. New York: W.H. Freeman and Company, 2002, 974 pp. ISBN 0-7167-4684-0. info
- NELSON, D.L. and M.M. COX. Lehninger Principles of Biochemistry. 3rd. New York: Worth Publishers, 2000, 1152 pp. ISBN 1-57259-153-6. info
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Teaching methods
- Series of lectures
- Assessment methods
- Lectures, abundantly documented with charts, diagrams, formulas and figures, which are offered to the students for making copies. Oral examination; 40 specified questions are at disposal.
- Language of instruction
- Czech
- Follow-Up Courses
- Further comments (probably available only in Czech)
- Study Materials
The course is taught annually.
Information on course enrolment limitations: Při týdenní výuce min. 8 posluchačů, při blokové bez omezení
C7150 Dynamic biochemistry I - control of metabolism
Faculty of ScienceAutumn 2008
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc. - Timetable
- Tue 9:00–10:50 C05/107
- Prerequisites
- Could be registered in the 3rd, 5th, 7th, 9th semester
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 26 fields of study the course is directly associated with, display
- Course objectives
- Dynamic biochemistry I - control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
Main objectives of the course can be summarized as follows:
to extend the knowledge of dynamic biochemistry and enzymology;
to get a view of the main metabolic pathways in bacteria and eukaryots;
to analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism;
to learn new information on biomedical aspects of biochemistry.
Overview of basic types of biochemical control mechanisms at the molecular level. Allosteric interactions, reversible covalent modifications of proteins, modulation of enzyme activities by regulatory proteins, proteolytic activation of zymogens. Control of metabolism at the level of whole organism. The coordination of catabolism and biosynthesis. - Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- STRYER, L. Biochemistry, 4th ed. New York: Freeman and Co., 1995, 1064 pp. info
- VOET, D. and J.G. VOET. Biochemistry, 2nd ed. New York: J. Wiley & Sons, 1995, 1361 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Assessment methods
- Lectures, abundantly documented with charts, diagrams, formulas and figures, which are offered to the students for making copies. Oral examination; 40 specified questions are at disposal.
- Language of instruction
- Czech
- Follow-Up Courses
- Further comments (probably available only in Czech)
- The course can also be completed outside the examination period.
The course is taught annually.
Information on course enrolment limitations: Při týdenní výuce min. 8 posluchačů, při blokové bez omezení
C7150 Metabolic pathways regulation
Faculty of ScienceAutumn 2007
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc. - Timetable
- Tue 9:00–10:50 C05/107
- Prerequisites (in Czech)
- Lze zapsat v 5.,7.,9. semestru po absolvování Biochemie II.
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 148 fields of study the course is directly associated with, display
- Course objectives
- An advanced lecture for MSc and PhD students of biochemistry and molecular biology or chemistry and general biology. Overview of basic types of biochemical control mechanisms at the molecular level. Allosteric interactions, reversible covalent modifications of proteins, modulation of enzyme activities by regulatory proteins, proteolytic activation of zymogens. Control of metabolism at the level of whole organism. The coordination of catabolism and biosynthesis.
- Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- STRYER, L. Biochemistry, 4th ed. New York: Freeman and Co., 1995, 1064 pp. info
- VOET, D. and J.G. VOET. Biochemistry, 2nd ed. New York: J. Wiley & Sons, 1995, 1361 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Language of instruction
- Czech
- Follow-Up Courses
- Further comments (probably available only in Czech)
- The course can also be completed outside the examination period.
The course is taught annually.
Information on course enrolment limitations: Při týdenní výuce min. 5 posluchačů, při blokové bez omezení
C7150 Regulace metabolických drah
Faculty of ScienceAutumn 2006
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc. - Timetable
- Tue 8:00–9:50 C04/211
- Prerequisites (in Czech)
- Lze zapsat v 5.,7.,9. semestru po absolvování Biochemie II.
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 43 fields of study the course is directly associated with, display
- Course objectives
- An advanced lecture for MSc and PhD students of biochemistry and molecular biology or chemistry and general biology. Overview of basic types of biochemical control mechanisms at the molecular level. Allosteric interactions, reversible covalent modifications of proteins, modulation of enzyme activities by regulatory proteins, proteolytic activation of zymogens. Control of metabolism at the level of whole organism. The coordination of catabolism and biosynthesis.
- Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- STRYER, L. Biochemistry, 4th ed. New York: Freeman and Co., 1995, 1064 pp. info
- VOET, D. and J.G. VOET. Biochemistry, 2nd ed. New York: J. Wiley & Sons, 1995, 1361 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Language of instruction
- Czech
- Follow-Up Courses
- Further Comments
- The course can also be completed outside the examination period.
The course is taught annually.
C7150 Regulace metabolických drah
Faculty of ScienceAutumn 2005
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc. - Timetable
- Wed 8:00–9:50 C02/121
- Prerequisites (in Czech)
- Lze zapsat v 5.,7.,9. semestru po absolvování Biochemie II.
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 43 fields of study the course is directly associated with, display
- Course objectives
- An advanced lecture for MSc and PhD students of biochemistry and molecular biology or chemistry and general biology. Overview of basic types of biochemical control mechanisms at the molecular level. Allosteric interactions, reversible covalent modifications of proteins, modulation of enzyme activities by regulatory proteins, proteolytic activation of zymogens. Control of metabolism at the level of whole organism. The coordination of catabolism and biosynthesis.
- Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- STRYER, L. Biochemistry, 4th ed. New York: Freeman and Co., 1995, 1064 pp. info
- VOET, D. and J.G. VOET. Biochemistry, 2nd ed. New York: J. Wiley & Sons, 1995, 1361 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Language of instruction
- Czech
- Follow-Up Courses
- Further Comments
- The course can also be completed outside the examination period.
The course is taught annually.
C7150 Regulace metabolických drah
Faculty of ScienceAutumn 2004
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc. - Timetable
- Wed 9:00–10:50 Cpm,02016
- Prerequisites (in Czech)
- Lze zapsat v 5.,7.,9. semestru po absolvování Biochemie II.
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 43 fields of study the course is directly associated with, display
- Course objectives
- An advanced lecture for MSc and PhD students of biochemistry and molecular biology or chemistry and general biology. Overview of basic types of biochemical control mechanisms at the molecular level. Allosteric interactions, reversible covalent modifications of proteins, modulation of enzyme activities by regulatory proteins, proteolytic activation of zymogens. Control of metabolism at the level of whole organism. The coordination of catabolism and biosynthesis.
- Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- STRYER, L. Biochemistry, 4th ed. New York: Freeman and Co., 1995, 1064 pp. info
- VOET, D. and J.G. VOET. Biochemistry, 2nd ed. New York: J. Wiley & Sons, 1995, 1361 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Language of instruction
- Czech
- Follow-Up Courses
- Further Comments
- The course can also be completed outside the examination period.
The course is taught annually.
C7150 Regulace metabolických drah
Faculty of ScienceAutumn 2003
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc. - Prerequisites (in Czech)
- Lze zapsat v 5.,7.,9. semestru po absolvování Biochemie II.
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 43 fields of study the course is directly associated with, display
- Course objectives
- An advanced lecture for MSc and PhD students of biochemistry and molecular biology or chemistry and general biology. Overview of basic types of biochemical control mechanisms at the molecular level. Allosteric interactions, reversible covalent modifications of proteins, modulation of enzyme activities by regulatory proteins, proteolytic activation of zymogens. Control of metabolism at the level of whole organism. The coordination of catabolism and biosynthesis.
- Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- STRYER, L. Biochemistry, 4th ed. New York: Freeman and Co., 1995, 1064 pp. info
- VOET, D. and J.G. VOET. Biochemistry, 2nd ed. New York: J. Wiley & Sons, 1995, 1361 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Language of instruction
- Czech
- Follow-Up Courses
- Further Comments
- The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: every week.
C7150 Regulace metabolických drah
Faculty of ScienceAutumn 2002
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc. - Prerequisites (in Czech)
- Lze zapsat v 5.,7.,9. semestru po absolvování Biochemie II.
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 43 fields of study the course is directly associated with, display
- Course objectives
- An advanced lecture for MSc and PhD students of biochemistry and molecular biology or chemistry and general biology. Overview of basic types of biochemical control mechanisms at the molecular level. Allosteric interactions, reversible covalent modifications of proteins, modulation of enzyme activities by regulatory proteins, proteolytic activation of zymogens. Control of metabolism at the level of whole organism. The coordination of catabolism and biosynthesis.
- Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- STRYER, L. Biochemistry, 4th ed. New York: Freeman and Co., 1995, 1064 pp. info
- VOET, D. and J.G. VOET. Biochemistry, 2nd ed. New York: J. Wiley & Sons, 1995, 1361 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Language of instruction
- Czech
- Follow-Up Courses
- Further Comments
- The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: every week.
C7150 Biochemical Regulations
Faculty of ScienceAutumn 2001
- Extent and Intensity
- 2/0/0. 3 credit(s). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Chemistry Section – Faculty of Science - Prerequisites (in Czech)
- C4182 Biochemistry II || C3580 Biochemistry
Lze zapsat v 5.,7.,9. sem. po absolvování Biochemie II, příp. i jako C7151! - Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 10 fields of study the course is directly associated with, display
- Course objectives
- Basic types of control mechanisms at the molecular and cellular levels. Mechanisms of hormonal actions; other signal molecules, receptors, transducing G-proteins; intracellular signal transduction pathways. Hormonal control of intermediary metabolism and complex physiological processes.
- Syllabus
- Survey of basic types of control mechanisms at the molecular level. Allosteric interactions, reversible covalent modifications of enzymes, regulatory proteins, proteolytic activation of zymogenes. Intercellular communication. Hormones and other signal molecules, receptors, transducing G-proteins, effectors and second messengers. Receptor tyrosine kinases, MAP kinase cascade. Convergence, divergence and crosstalk of signal transduction pathways. GTPases as molecular switches. Receptor desensitization, "receptor diseases", hormonal control of complex physiological processes.
- Literature
- Ca. 200 blan k dispozici u přednášejícího.
- Language of instruction
- Czech
- Further Comments
- The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: every week.
C7150 Biochemical Regulations
Faculty of ScienceAutumn 2000
- Extent and Intensity
- 2/0/0. 3 credit(s). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Chemistry Section – Faculty of Science - Prerequisites (in Czech)
- C4182 Biochemistry II || C3580 Biochemistry
Lze zapsat v 5.,7.,9. sem. po absolvování Biochemie II, příp. i jako C7151! - Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 10 fields of study the course is directly associated with, display
- Course objectives
- Basic types of control mechanisms at the molecular and cellular levels. Mechanisms of hormonal actions; other signal molecules, receptors, transducing G-proteins; intracellular signal transduction pathways. Hormonal control of intermediary metabolism and complex physiological processes.
- Syllabus
- Survey of basic types of control mechanisms at the molecular level. Allosteric interactions, reversible covalent modifications of enzymes, regulatory proteins, proteolytic activation of zymogenes. Intercellular communication. Hormones and other signal molecules, receptors, transducing G-proteins, effectors and second messengers. Receptor tyrosine kinases, MAP kinase cascade. Convergence, divergence and crosstalk of signal transduction pathways. GTPases as molecular switches. Receptor desensitization, "receptor diseases", hormonal control of complex physiological processes.
- Literature
- Ca. 200 blan k dispozici u přednášejícího.
- Language of instruction
- Czech
- Further Comments
- The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: every week.
C7150 Biochemical Regulations
Faculty of ScienceAutumn 1999
- Extent and Intensity
- 2/2/0. 5 credit(s). Type of Completion: zk (examination).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Chemistry Section – Faculty of Science - Prerequisites (in Czech)
- Lze zapsat v 5.,7.,9. sem. po absolvování Biochemie II, příp. i jako C7151!
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Biochemistry (programme PřF, M-CH)
- Biochemistry (programme PřF, N-CH)
- Syllabus
- Survey of basic types of control mechanisms at the molecular level. Allosteric interactions, reversible covalent modifications of enzymes, regulatory proteins, proteolytic activation of zymogenes. Intercellular communication. Hormones and other signal molecules, receptors, transducing G-proteins, effectors and second messengers. Receptor tyrosine kinases, MAP kinase cascade. Convergence, divergence and crosstalk of signal transduction pathways. GTPases as molecular switches. Receptor desensitization, "receptor diseases", hormonal control of complex physiological processes.
- Literature
- Ca. 200 blan k dispozici u přednášejícího.
- Language of instruction
- Czech
- Further Comments
- The course is taught annually.
The course is taught: every week.
C7150 Dynamic biochemistry I - control of metabolism
Faculty of ScienceAutumn 2011 - acreditation
The information about the term Autumn 2011 - acreditation is not made public
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc. - Prerequisites
- Could be registered in the 3rd, 5th, 7th, 9th semester
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 20 fields of study the course is directly associated with, display
- Course objectives
- Dynamic biochemistry I - control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
Learning outcomes:
At the end of the course, students should be able to:
- describe and explain the main metabolic pathways in bacteria and eukaryots;
- analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism;
- reproduce and present their extended knowledge of dynamic biochemistry and enzymology;
- demonstrate new information on biomedical aspects of biochemistry. - Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- STOREY, K.B. (ed.). Functional Metabolism: Regulation and Adaptation. Hoboken, New Jersey: Wiley-Liss, Inc., 2004, 594 pp. ISBN 0-471-41090-X. info
- Biochemistry. Edited by Donald Voet - Judith G. Voet. 3rd ed. Hoboken, N.J.: John Wiley & Sons, 2004, xv, 1591 s. ISBN 0-471-41761-0. info
- BERG, J.M., J.L. TYMOCZKO and L. STRYER. Biochemistry. 5th. New York: W.H. Freeman and Company, 2002, 974 pp. ISBN 0-7167-4684-0. info
- NELSON, D.L. and M.M. COX. Lehninger Principles of Biochemistry. 3rd. New York: Worth Publishers, 2000, 1152 pp. ISBN 1-57259-153-6. info
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Teaching methods
- Series of lectures
- Assessment methods
- Lectures, abundantly documented with charts, diagrams, formulas and figures, which are offered to the students for making copies. Oral examination; 40 specified questions are at disposal.
- Language of instruction
- Czech
- Follow-Up Courses
- Further comments (probably available only in Czech)
- The course is taught annually.
The course is taught: every week.
Note related to how often the course is taught: blokově.
Information on course enrolment limitations: Při týdenní výuce min. 8 posluchačů, při blokové bez omezení
C7150 Dynamic biochemistry I - control of metabolism
Faculty of ScienceAutumn 2010 - only for the accreditation
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc. - Prerequisites
- Could be registered in the 3rd, 5th, 7th, 9th semester
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 20 fields of study the course is directly associated with, display
- Course objectives
- Dynamic biochemistry I - control of metabolism. A follow-up lecture course of dynamic biochemistry and pathobiochemistry for MSc (and also PhD) and Bc students of biochemistry and molecular biology and also of general biology, chemistry and medicine.
Learning outcomes:
At the end of the course, students should be able to:
- describe and explain the main metabolic pathways in bacteria and eukaryots;
- analyze the control mechanisms engaged in the coordination of catabolic and anabolic processes at the level of whole organism;
- reproduce and present their extended knowledge of dynamic biochemistry and enzymology;
- demonstrate new information on biomedical aspects of biochemistry. - Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- STOREY, K.B. (ed.). Functional Metabolism: Regulation and Adaptation. Hoboken, New Jersey: Wiley-Liss, Inc., 2004, 594 pp. ISBN 0-471-41090-X. info
- Biochemistry. Edited by Donald Voet - Judith G. Voet. 3rd ed. Hoboken, N.J.: John Wiley & Sons, 2004, xv, 1591 s. ISBN 0-471-41761-0. info
- BERG, J.M., J.L. TYMOCZKO and L. STRYER. Biochemistry. 5th. New York: W.H. Freeman and Company, 2002, 974 pp. ISBN 0-7167-4684-0. info
- NELSON, D.L. and M.M. COX. Lehninger Principles of Biochemistry. 3rd. New York: Worth Publishers, 2000, 1152 pp. ISBN 1-57259-153-6. info
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Teaching methods
- Series of lectures
- Assessment methods
- Lectures, abundantly documented with charts, diagrams, formulas and figures, which are offered to the students for making copies. Oral examination; 40 specified questions are at disposal.
- Language of instruction
- Czech
- Follow-Up Courses
- Further comments (probably available only in Czech)
- The course is taught annually.
The course is taught: every week.
Note related to how often the course is taught: blokově.
Information on course enrolment limitations: Při týdenní výuce min. 8 posluchačů, při blokové bez omezení
C7150 Regulace metabolických drah
Faculty of ScienceAutumn 2007 - for the purpose of the accreditation
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Stanislav Pavelka, CSc. (lecturer)
- Guaranteed by
- doc. RNDr. Stanislav Pavelka, CSc.
Department of Biochemistry – Chemistry Section – Faculty of Science
Contact Person: doc. RNDr. Stanislav Pavelka, CSc. - Prerequisites (in Czech)
- Lze zapsat v 5.,7.,9. semestru po absolvování Biochemie II.
- Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- there are 43 fields of study the course is directly associated with, display
- Course objectives
- An advanced lecture for MSc and PhD students of biochemistry and molecular biology or chemistry and general biology. Overview of basic types of biochemical control mechanisms at the molecular level. Allosteric interactions, reversible covalent modifications of proteins, modulation of enzyme activities by regulatory proteins, proteolytic activation of zymogens. Control of metabolism at the level of whole organism. The coordination of catabolism and biosynthesis.
- Syllabus
- I. Biochemical regulations at the molecular level. 1. Overview of the basic types of biochemical regulation mechanisms. 2. Allosteric regulations - generally. (Models of allosteric interactions - concerted (symmetrical model) and sequential. Cooperative binding, homotropic and heterotropic interactions). 3. Hemoglobin (Hb) as a prototype of an allosteric protein. (Biological function of Hb, differences between Hb and myoglobin. Changes in quaternary structure of Hb on oxygenation. The Bohr effect - the influence of H+ and CO2 concentrations on the affinity of hemoglobin for oxygen. The effect of 2,3-bisphosphoglycerate on the binding of oxygen by Hb). 4. Allosteric control of enzyme activity of aspartate transcarbamoylase (ATCase). (The function of ATCase, biological significance of the allosteric regulation. Dissociation of catalytic and regulatory subunits of ATCase. Structural basis of allosteric interactions in ATCase). 5. Regulation of bacterial biosynthesis of aminoacids. (Types of feedback inhibition of branched metabolic pathways). 6. Reversible covalent modification of enzymes. (The role of phosphorylation and dephosphorylation reactions in control processes. Modulation of glutamine synthetase activity by reversible covalent modification). 7. Modulation of enzyme activity by regulatory proteins. (Control of covalent modification of glutamine synthetase by enzyme cascade). 8. Activation of zymogens by specific proteolytic cleavage. (Activation of trypsinogen and chymotrypsinogen. The cascade of proteolytic activation of zymogens in the process of blood clotting. The role for vitamin K in the biosynthesis of prothrombin. Complex regulation of blood clotting). II. Control of metabolism at the level of whole organism. 9. Overview of the metabolic pathways. (From the macromolecules of food to ATP). 10. Glycolysis. (Allosteric control of key enzymes in glycolysis). 11. Regulation of the metabolism of glycogen. (Overview of the reactions of glycogen biosynthesis and breakdown. Structural basis of the control of enzymes engaged in glycogen metabolism. Integration of control mechanisms - maintaining the blood glucose level constant). 12. Citric acid cycle. The respiratory chain and oxidative phosphorylation. 13. Regulation of ATP synthesis. (ATP synthase. Adenine nucleotide translocase. Na+,K+ -ATPase as an example of ionic pump).
- Literature
- GARRETT, R.H. and C.M. GRISHAM. Biochemistry, 2nd ed. Fort Worth, Orlando: Saunders College Publ., 1999, 1127 pp. info
- STRYER, L. Biochemistry, 4th ed. New York: Freeman and Co., 1995, 1064 pp. info
- VOET, D. and J.G. VOET. Biochemistry, 2nd ed. New York: J. Wiley & Sons, 1995, 1361 pp. info
- Ca. 200 blan k dispozici u přednášejícího.
- Language of instruction
- Czech
- Follow-Up Courses
- Further Comments
- The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: every week.
- Enrolment Statistics (recent)