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Converting an Esterase into an Epoxide Hydrolase
Author(s) -
Jochens Helge,
Stiba Konstanze,
Savile Christopher,
Fujii Ryota,
Yu JuinGuo,
Gerassenkov Tatsiana,
Kazlauskas Romas J.,
Bornscheuer Uwe T.
Publication year - 2009
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.200806276
Subject(s) - epoxide hydrolase , esterase , hydrolase , chemistry , epoxide , enzyme , stereochemistry , biochemistry , hydrolysis , epoxide hydrolase 2 , enantioselective synthesis , catalysis , microsome
Entering the fold : A common structural motif in hydrolytic enzymes is the α,β‐hydrolase fold. The interconversion of one enzyme into another by introduction of mechanistically important residues is not enough; only substitution of a loop allows epoxide hydrolase activity in the esterase scaffold to be formed (see picture; structure comparison of epoxide hydrolases (green) with the esterase (orange)). The result is an enantioselective chimeric enzyme.