Detailed Information on Publication Record
2017
Structure-function Relationships and Engineering of Haloalkane Dehalogenases.
KOKKONEN, Piia Pauliina, Táňa KOUDELÁKOVÁ, Radka CHALOUPKOVÁ, Lukáš DANIEL, Zbyněk PROKOP et. al.Basic information
Original name
Structure-function Relationships and Engineering of Haloalkane Dehalogenases.
Authors
KOKKONEN, Piia Pauliina (246 Finland, belonging to the institution), Táňa KOUDELÁKOVÁ (203 Czech Republic, belonging to the institution), Radka CHALOUPKOVÁ (203 Czech Republic, belonging to the institution), Lukáš DANIEL (203 Czech Republic, belonging to the institution), Zbyněk PROKOP (203 Czech Republic, belonging to the institution) and Jiří DAMBORSKÝ (203 Czech Republic, guarantor, belonging to the institution)
Edition
Heidelberg, HANDBOOK OF HYDROCARBON AND LIPID MICROBIOLOGY SERIES. AEROBIC UTILIZATION OF HYDROCARBONS, OILS, AND LIPIDS, p. 1-21, 21 pp. 2017
Publisher
Springer, Cham
Other information
Language
English
Type of outcome
Kapitola resp. kapitoly v odborné knize
Field of Study
10608 Biochemistry and molecular biology
Country of publisher
Switzerland
Confidentiality degree
není předmětem státního či obchodního tajemství
Publication form
electronic version available online
References:
RIV identification code
RIV/00216224:14310/17:00100792
Organization unit
Faculty of Science
ISBN
978-3-319-50419-3
Keywords in English
Biodegradation Hydrocarbons Bacteria Yeasts Alkanes Gasoline Aromatic hydrocarbons Degradation of lipids Fatty acids
Tags
Změněno: 5/3/2019 13:15, prof. Mgr. Jiří Damborský, Dr.
Abstract
V originále
The structure-function relationships for haloalkane dehalogenases, one of the best characterized enzyme families involved in degradation of halogenated compounds, is described. A substantial amount of mechanistic and structural information is currently available on haloalkane dehalogenases, providing good theoretical framework for their modification by protein engineering. Examples of constructed mutants include variants with modified: (i) activity and specificity, (ii) stability, and (ii) enantioselectivity. Many variants carried mutations in the tunnels connecting the buried active site with surrounding solvent, rather than in the active site itself. Mutagenesis of residues lining the protein tunnels represents attractive and a viable approach of protein engineering.
Links
GA16-06096S, research and development project |
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GA16-07965S, research and development project |
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GA16-24223S, research and development project |
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LM2015047, research and development project |
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LM2015051, research and development project |
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LM2015055, research and development project |
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LO1214, research and development project |
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