Structural highlights
FunctionPublication Abstract from PubMedFlavoprotein monooxygenases are a versatile group of enzymes for biocatalytic transformations. Among these, group E monooxygenases (GEMs) catalyze enantioselective epoxidation and sulfoxidation reactions. Here, we describe the crystal structure of an indole monooxygenase from the bacterium Variovorax paradoxus EPS, a GEM designated as VpIndA1. Complex structures with substrates reveal productive binding modes that, in conjunction with force-field calculations and rapid mixing kinetics, reveal the structural basis of substrate and stereoselectivity. Structure-based redesign of the substrate cavity yielded variants with new substrate selectivity (for sulfoxidation of benzyl phenyl sulfide) or with greatly enhanced stereospecificity (from 35.1 % to 99.8 % ee for production of (1S,2R) indene oxide). This first determination of the substrate binding mode of GEMs combined with structure-function relationships opens the door for structure-based design of these powerful biocatalysts. Structural and Mechanistical Studies on Substrate and Stereo Selectivity of the Indole Monooxygenase VpIndA1: New Avenues for Biocatalytic Epoxidations and Sulfoxidations.,Kratky J, Eggerichs D, Heine T, Hofmann S, Sowa P, Weisse RH, Tischler D, Strater N Angew Chem Int Ed Engl. 2023 Feb 10:e202300657. doi: 10.1002/anie.202300657. PMID:36762980[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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