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.

Other information

• Original 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: http://dx.doi.org/10.1002/anie.201206708
• UT WoS: 000314654000011
• Keywords in English: haloalkan dehalogenases
• Tags: AKR, rivok
• Tags: International impact, Reviewed

Abstract

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)