Engineering Enzyme Stability and Resistance to an Organic Cosolvent by Modification of Residues in the Access Tunnel

KOUDELÁKOVÁ, Táňa, Radka CHALOUPKOVÁ, Jan BREZOVSKÝ, Zbyněk PROKOP, Eva ŠEBESTOVÁ, M. HESSELER, M. KHABIRI, M. PLEVAKA, D. KULIK, I. KUTA SMATANOVA, P. REZACOVA, R. ETTRICH, U.T. BORNSCHEUER and Jiří DAMBORSKÝ. Engineering Enzyme Stability and Resistance to an Organic Cosolvent by Modification of Residues in the Access Tunnel. Angewandte Chemie International Edition. Verlag Chemie, 2013, vol. 52, No 7, p. 1959-1963. ISSN 1433-7851. Available from: https://dx.doi.org/10.1002/anie.201206708.

Basic information

Original name

Engineering Enzyme Stability and Resistance to an Organic Cosolvent by Modification of Residues in the Access Tunnel

Authors

KOUDELÁKOVÁ, Táňa (203 Czech Republic, belonging to the institution), Radka CHALOUPKOVÁ (203 Czech Republic, belonging to the institution), Jan BREZOVSKÝ (203 Czech Republic, belonging to the institution), Zbyněk PROKOP (203 Czech Republic, belonging to the institution), Eva ŠEBESTOVÁ (203 Czech Republic, belonging to the institution), M. HESSELER (203 Czech Republic), M. KHABIRI (364 Islamic Republic of Iran), M. PLEVAKA (203 Czech Republic), D. KULIK (203 Czech Republic), I. KUTA SMATANOVA (203 Czech Republic), P. REZACOVA (203 Czech Republic), R. ETTRICH (276 Germany), U.T. BORNSCHEUER (276 Germany) and Jiří DAMBORSKÝ (203 Czech Republic, guarantor, belonging to the institution)

Edition

Angewandte Chemie International Edition, Verlag Chemie, 2013, 1433-7851

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Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

Germany

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 11.336

RIV identification code

RIV/00216224:14310/13:00066682

Organization unit

Faculty of Science

DOI

http://dx.doi.org/10.1002/anie.201206708

UT WoS

000314654000011

Keywords in English

haloalkan dehalogenases

Tags

AKR, rivok

Tags

International impact, Reviewed

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Abstract

V originále

Mutations targeting as few as four residues lining the access tunnel extended enzyme’s half-life in 40% dimethyl sulfoxide from minutes to weeks (4,000-fold) and increased its melting temperature by 19 Grades C. Protein crystallography and molecular dynamics revealed that the tunnel residue packing is a key determinant of protein stability and the active-site accessibility for co-solvent molecules (red dots). The broad applicability of this concept was verified by analyzing twenty six proteins with buried active sites from all six enzyme classes.

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Links

ED0001/01/01, research and development project	Name: CETOCOEN
GAP202/10/1435, research and development project	Name: Analýza a vizualizace proteinových struktur Investor: Czech Science Foundation, Analysis and Visualization of Protein Structures
GAP207/12/0775, research and development project	Name: Strukturně-funkční vztahy haloalkan dehalogenas Investor: Czech Science Foundation
GA203/08/0114, research and development project	Name: Specifické iontové efekty pro proteiny v roztocích a podobné biologicky relevantní systémy. Investor: Czech Science Foundation, Specific ion effects for proteins in solutions and related biologically relevant systems
LC06010, research and development project	Name: Centrum biokatalýzy a biotransformací Investor: Ministry of Education, Youth and Sports of the CR, Center of Biocatalysis and Biotransformation
MSM0021622412, plan (intention)	Name: Interakce mezi chemickými látkami, prostředím a biologickými systémy a jejich důsledky na globální, regionální a lokální úrovni (INCHEMBIOL) (Acronym: INCHEMBIOL) Investor: Ministry of Education, Youth and Sports of the CR, Interactions among the chemicals, environment and biological systems and their consequences on the global, regional and local scales (INCHEMBIOL)