C 2019

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, 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

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

printed version "print"

References:

RIV identification code

RIV/00216224:14310/19:00119131

Organization unit

Faculty of Science

ISBN

978-3-319-50417-9

UT WoS

000623123900015

Keywords in English

haloalkane dehalogenase; protein engineering

Tags

International impact, Reviewed
Změněno: 16/8/2021 13:12, Mgr. Marie Šípková, DiS.

Abstract

V originále

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.

Links

GA16-06096S, research and development project
Name: Objasnění významu dynamických tunelů pro enzymatickou katalýzu: simulace a fluorescenční experimenty
Investor: Czech Science Foundation
GA16-07965S, research and development project
Name: Řízená evoluce dynamických elementů v enzymech s využitím mikrofluidních čipů
Investor: Czech Science Foundation
GA16-24223S, research and development project
Name: Strukturní podstata vzniku nových enzymových aktivit
Investor: Czech Science Foundation
LM2015051, research and development project
Name: Centrum pro výzkum toxických látek v prostředí (Acronym: RECETOX RI)
Investor: Ministry of Education, Youth and Sports of the CR
LM2015055, research and development project
Name: Centrum pro systémovou biologii (Acronym: C4SYS)
Investor: Ministry of Education, Youth and Sports of the CR
LM2015085, research and development project
Name: CERIT Scientific Cloud (Acronym: CERIT-SC)
Investor: Ministry of Education, Youth and Sports of the CR, CERIT Scientific Cloud
LO1214, research and development project
Name: Centrum pro výzkum toxických látek v prostředí (Acronym: RECETOX)
Investor: Ministry of Education, Youth and Sports of the CR
676559, interní kód MU
Name: 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 infrastructures
Name: CESNET II