PřF:C7150 Dynamic biochemistry I-metabol - Course Information
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
- Enrolment Statistics (Autumn 2014, recent)
- Permalink: https://is.muni.cz/course/sci/autumn2014/C7150