C 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
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
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
LM2015047, research and development project
Name: Česká národní infrastruktura pro biologická data (Acronym: ELIXIR-CZ)
Investor: Ministry of Education, Youth and Sports of the CR, Czech National Infrastructure for Biological Data
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
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