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

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Authors	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
Year of publication	2013
Type	Article in Periodical
Magazine / Source	Angewandte Chemie International Edition
MU Faculty or unit	Faculty of Science
Citation
Doi	https://doi.org/10.1002/anie.201206708
Field	Biochemistry
Keywords	haloalkan dehalogenases
Description	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.
Related projects:	Interactions among the chemicals, environment and biological systems and their consequences on the global, regional and local scales (INCHEMBIOL) Center of Biocatalysis and Biotransformation Specific ion effects for proteins in solutions and related biologically relevant systems Analysis and Visualization of Protein Structures Centrum pro výzkum toxických látek v prostředí Structure-functional Relationships of Haloalkane Dehalogenases