Journal
ACS CHEMICAL BIOLOGY
Volume 9, Issue 12, Pages 2843-2851Publisher
AMER CHEMICAL SOC
DOI: 10.1021/cb500442e
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Funding
- Natural Sciences and Engineering Research Council of Canada ( [NSERC RGPIN 183867-13]
- Canadian Institute of Health Research [CIHR MOP-114889]
- Natural Sciences and Engineering Research Council of Canada
- McGill University
- CIHR Strategic Initiative in Chemical Biology
- NSERC CREATE Program in Bionanomachines
- Canada Research Chair in Structural Biology
- Fonds quebecois de la recherche sur la nature et les technologies Center for Green Chemistry and Catalysis
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The BaeyerVilliger monooxygenases (BVMOs) are microbial enzymes that catalyze the synthetically useful BaeyerVilliger oxidation reaction. The available BVMO crystal structures all lack a substrate or product bound in a position that would determine the substrate specificity and stereospecificity of the enzyme. Here, we report two crystal structures of cyclohexanone monooxygenase (CHMO) with its product, e-caprolactone, bound: the CHMOTight and CHMOLoose structures. The CHMOTight structure represents the enzyme state in which substrate acceptance and stereospecificity is determined, providing a foundation for engineering BVMOs with altered substrate spectra and/or stereospecificity. The CHMOLoose structure is the first structure where the product is solvent accessible. This structure represents the enzyme state upon binding and release of the substrate and product. In addition, the role of the invariant Arg329 in chaperoning the substrate/product during the catalytic cycle is highlighted. Overall, these data provide a structural framework for the engineering of BVMOs with altered substrate spectra and/or stereospecificity.
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