Erratum: Converting an esterase into an epoxide hydrolase

Helge Jochens, Konstanze Stiba, Christopher Savile, Ryota Fujii, Juin Guo Yu, Tatsiana Gerassenkov, Romas J. Kazlauskas, Uwe T. Bornscheuer

Research output: Contribution to journalArticlepeer-review

58 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)3532-3535
Number of pages4
JournalAngewandte Chemie - International Edition
Volume48
Issue number19
DOIs
StatePublished - Apr 27 2009

Keywords

  • Directed evolution
  • Enantioselectivity
  • Enzyme catalysis
  • Epoxide hydrolases
  • Esterases

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