Catalytic Promiscuity in Biocatalysis: Using Old Enzymes to Form New Bonds and Follow New Pathways

TLDR

Biocatalysis has rapidly expanded, with highly stereoselective enzymes of broad substrate specificity, and a new frontier is broad reaction specificity where enzymes catalyze alternate reactions, reflecting catalytic promiscuity’s natural evolutionary role and occasional contribution to secondary metabolite biosynthesis. The study reviews examples of catalytic promiscuity with current or potential applications in synthesis. The authors review catalytic promiscuity examples to illustrate their applications in synthesis. Combined with protein engineering, catalytic promiscuity may broadly extend enzyme usefulness in organic synthesis.

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.