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

J 2013

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 et. al.

Basic information

Original name

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

Authors

Edition

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

Other information

Language

English

Type of outcome

Article in a journal

Field of Study

10600 1.6 Biological sciences

Country of publisher

Germany

Confidentiality degree

is not subject to a state or trade secret

Impact factor

Impact factor: 11.336

RIV identification code

RIV/00216224:14310/13:00066682

Organization unit

Faculty of Science

DOI

https://doi.org/10.1002/anie.201206708

UT WoS

000314654000011

Keywords in English

haloalkan dehalogenases

Abstract

In the original language

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.

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)

Cite

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

@article{1138880,
   author = {Koudeláková, Táňa and Chaloupková, Radka and Brezovský, Jan and Prokop, Zbyněk and Šebestová, Eva and Hesseler, M. and Khabiri, M. and Plevaka, M. and Kulik, D. and Kuta Smatanova, I. and Rezacova, P. and Ettrich, R. and Bornscheuer, U.T. and Damborský, Jiří},
   article_number = {7},
   doi = {https://doi.org/10.1002/anie.201206708},
   keywords = {haloalkan dehalogenases},
   language = {eng},
   issn = {1433-7851},
   journal = {Angewandte Chemie International Edition},
   title = {Engineering Enzyme Stability and Resistance to an Organic Cosolvent by Modification of Residues in the Access Tunnel},
   volume = {52},
   year = {2013}
}

TY  - JOUR
ID  - 1138880
AU  - Koudeláková, Táňa - Chaloupková, Radka - Brezovský, Jan - Prokop, Zbyněk - Šebestová, Eva - Hesseler, M. - Khabiri, M. - Plevaka, M. - Kulik, D. - Kuta Smatanova, I. - Rezacova, P. - Ettrich, R. - Bornscheuer, U.T. - Damborský, Jiří
PY  - 2013
TI  - Engineering Enzyme Stability and Resistance to an Organic Cosolvent by Modification of Residues in the Access Tunnel
JF  - Angewandte Chemie International Edition
VL  - 52
IS  - 7
SP  - 1959-1963
EP  - 1959-1963
PB  - Verlag Chemie
SN  - 14337851
KW  - haloalkan dehalogenases
N2  - 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.
ER  -

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. \textit{Angewandte Chemie International Edition}. Verlag Chemie, 2013, vol.~52, No~7, p.~1959-1963. ISSN~1433-7851. Available from: https://doi.org/10.1002/anie.201206708.

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