Format

Send to

Choose Destination
Angew Chem Int Ed Engl. 2004 Nov 19;43(45):6032-40.

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

Author information

1
Institute of Chemistry and Biochemistry, Department of Technical Chemistry and Biotechnology, Greifswald University, Soldmannstrasse 16, 17487 Greifswald, Germany. uwe.bornscheuer@uni-greifswald.de

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 under-appreciated, 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.

PMID:
15523680
DOI:
10.1002/anie.200460416
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center