Catalytic promiscuity in biocatalysis: Using old enzymes to form new bonds and follow new pathways

Uwe T. Bornscheuer, Romas J. Kazlauskas

Research output: Contribution to journalShort surveypeer-review

449 Scopus citations

Abstract

Biocatalysis has expanded rapidly in the last decades with the discoveries of highly stereoselective enzymes with broad substrate specificity. A new frontier for biocatalysis is broad reaction specificity, where enzymes catalyze alternate reactions. Although often underappreciated, catalytic promiscuity has a natural role in evolution and occasionally in the biosynthesis of secondary metabolites. Examples of catalytic promiscuity with current or potential applications in synthesis are reviewed here. Combined with protein engineering, the catalytic promiscuity of enzymes may broadly extend their usefulness in organic synthesis.

Original languageEnglish (US)
Pages (from-to)6032-6040
Number of pages9
JournalAngewandte Chemie - International Edition
Volume43
Issue number45
DOIs
StatePublished - Nov 19 2004

Keywords

  • Biosynthesis
  • Biotransformations
  • Enzyme catalysis
  • Molecular modeling
  • Proteins

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