Enantiocomplementary enzymes: Classification, molecular basis for their enantiopreference, and prospects for mirror-image biotransformations

Paul F. Mugford, Ulrike G. Wagner, Yun Jiang, Kurt Faber, Romas J. Kazlauskas

Research output: Contribution to journalShort surveypeer-review

81 Scopus citations

Abstract

One often-cited weakness of biocatalysis is the lack of mirror-image enzymes for the formation of either enantiomer of a product in asymmetric synthesis. Enantiocomplementary enzymes exist as the solution to this problem in nature. These enzyme pairs, which catalyze the same reaction but favor opposite enantiomers, are not mirror-image molecules; however, they contain active sites that are functionally mirror images of one another. To create mirror-image active sites, nature can change the location of the binding site and/or the location of key catalytic groups. In this Minireview, X-ray crystal structures of enantiocomplementary enzymes are surveyed and classified into four groups according to how the mirror-image active sites are formed.

Original languageEnglish (US)
Pages (from-to)8782-8793
Number of pages12
JournalAngewandte Chemie - International Edition
Volume47
Issue number46
DOIs
StatePublished - Nov 3 2008

Keywords

  • Asymmetric synthesis
  • Biotransformations
  • Enantioselectivity
  • Protein engineering
  • Protein structures

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