Converting an Esterase into an Epoxide Hydrolase

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...

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Veröffentlicht in:Angewandte Chemie (International ed.) 2009-01, Vol.48 (19), p.3532-3535
Hauptverfasser: Jochens, Helge, Stiba, Konstanze, Savile, Christopher, Fujii, Ryota, Yu, Juin-Guo, Gerassenkov, Tatsiana, Kazlauskas, Romas J, Bornscheuer, Uwe T
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Sprache:eng
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Zusammenfassung: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.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200806276