KOKKONEN, Piia Pauliina, Táňa KOUDELÁKOVÁ, Radka CHALOUPKOVÁ, Lukáš DANIEL, Zbyněk PROKOP and Jiří DAMBORSKÝ. Structure-Function Relationships and Engineering of Haloalkane Dehalogenases. In Aerobic Utilization of Hydrocarbons, Oils, and Lipids. Cham: Springer, 2019, p. 367-387. 1. ISBN 978-3-319-50417-9. Available from: https://dx.doi.org/10.1007/978-3-319-50418-6_15.
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Basic information
Original name Structure-Function Relationships and Engineering of Haloalkane Dehalogenases
Authors KOKKONEN, Piia Pauliina (246 Finland, guarantor, 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, belonging to the institution).
Edition Cham, Aerobic Utilization of Hydrocarbons, Oils, and Lipids, p. 367-387, 21 pp. 1. 2019.
Publisher Springer
Other information
Original language English
Type of outcome Chapter(s) of a specialized book
Field of Study 10608 Biochemistry and molecular biology
Country of publisher Switzerland
Confidentiality degree is not subject to a state or trade secret
Publication form printed version "print"
WWW URL
RIV identification code RIV/00216224:14310/19:00119131
Organization unit Faculty of Science
ISBN 978-3-319-50417-9
Doi http://dx.doi.org/10.1007/978-3-319-50418-6_15
UT WoS 000623123900015
Keywords in English haloalkane dehalogenase; protein engineering
Tags topvydavatel
Tags International impact, Reviewed
Changed by Changed by: Mgr. Marie Šípková, DiS., učo 437722. Changed: 16/8/2021 13:12.
Abstract
The structure-function relationships for haloalkane dehalogenases, one of the best characterized enzyme families involved in degradation of halogenated compounds, are 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.
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GA16-06096S, research and development projectName: Objasnění významu dynamických tunelů pro enzymatickou katalýzu: simulace a fluorescenční experimenty
Investor: Czech Science Foundation
GA16-07965S, research and development projectName: Řízená evoluce dynamických elementů v enzymech s využitím mikrofluidních čipů
Investor: Czech Science Foundation
GA16-24223S, research and development projectName: Strukturní podstata vzniku nových enzymových aktivit
Investor: Czech Science Foundation
LM2015051, research and development projectName: Centrum pro výzkum toxických látek v prostředí (Acronym: RECETOX RI)
Investor: Ministry of Education, Youth and Sports of the CR
LM2015055, research and development projectName: Centrum pro systémovou biologii (Acronym: C4SYS)
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LM2015085, research and development projectName: CERIT Scientific Cloud (Acronym: CERIT-SC)
Investor: Ministry of Education, Youth and Sports of the CR, CERIT Scientific Cloud
LO1214, research and development projectName: Centrum pro výzkum toxických látek v prostředí (Acronym: RECETOX)
Investor: Ministry of Education, Youth and Sports of the CR
676559, interní kód MUName: ELIXIR-EXCELERATE: Fast-track ELIXIR implementation and drive early user exploitation across the life-sciences (Acronym: ELIXIR-EXCELERATE)
Investor: European Union, RI Research Infrastructures (Excellent Science)
90042, large research infrastructuresName: CESNET II
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