Converting an Esterase into an Epoxide Hydrolase (pages 3532–3535)
Helge Jochens, Konstanze Stiba, Christopher Savile, Ryota Fujii, Juin-Guo Yu, Tatsiana Gerassenkov, Romas J. Kazlauskas and Uwe T. Bornscheuer
Article first published online: 6 APR 2009 | DOI: 10.1002/anie.200806276
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.