Catalytic promiscuity in biocatalysis: using old enzymes to form new bonds and follow new pathways.
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.
Bornscheuer
Uwe T
UT
Institute of Chemistry and Biochemistry, Department of Technical Chemistry and Biotechnology, Greifswald University, Soldmannstrasse 16, 17487 Greifswald, Germany. uwe.bornscheuer@uni-greifswald.de
Kazlauskas
Romas J
RJ
D001709:Biotechnology / Q000379:methods; D002384:Catalysis; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism; D015394:Molecular Structure; D015202:Protein Engineering; D011506:Proteins / Q000737:chemistry / Q000378:metabolism
D004798:Enzymes; D011506:Proteins