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Engineering Enzyme Stability and Resistance to an Organic Cosolvent by Modification of Residues in the Access Tunnel
Author(s) -
Koudelakova Tana,
Chaloupkova Radka,
Brezovsky Jan,
Prokop Zbynek,
Sebestova Eva,
Hesseler Martin,
Khabiri Morteza,
Plevaka Maryia,
Kulik Daryna,
Kuta Smatanova Ivana,
Rezacova Pavlina,
Ettrich Rudiger,
Bornscheuer Uwe T.,
Damborsky Jiri
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201206708
Subject(s) - residue (chemistry) , dimethyl sulfoxide , enzyme , protein engineering , molecule , chemistry , molecular dynamics , melting temperature , stereochemistry , combinatorial chemistry , materials science , organic chemistry , computational chemistry , composite material
Mutations targeting as few as four residues lining the access tunnel extended the half‐life of an enzyme in 40 % dimethyl sulfoxide from minutes to weeks and increased its melting temperature by 19 °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 cosolvent molecules (red dots).