5m0z

Cyclohexanone Monooxygenase from T. municipale: reduced enzyme bound to NADP+

spinqualitylabelsall models 5m0z, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5m0z is a 1 chain structure with sequence from Thermocrispum municipale DSM 44069. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: FAD, GOL, NA7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1L1QK39_9PSEU Publication Abstract from PubMed Cyclohexanone monooxygenase (CHMO) is a promising biocatalyst for industrial reactions owing to its broad substrate spectrum and excellent regio-, chemo-, and enantioselectivity. However, the low stability of many Baeyer-Villiger monooxygenases is an obstacle for their exploitation in industry. Characterization and crystal structure determination of a robust CHMO from Thermocrispum municipale is reported. The enzyme efficiently converts a variety of aliphatic, aromatic, and cyclic ketones, as well as prochiral sulfides. A compact substrate-binding cavity explains its preference for small rather than bulky substrates. Small-scale conversions with either purified enzyme or whole cells demonstrated the remarkable properties of this newly discovered CHMO. The exceptional solvent tolerance and thermostability make the enzyme very attractive for biotechnology. Characterization and Crystal Structure of a Robust Cyclohexanone Monooxygenase.,Romero E, Castellanos JR, Mattevi A, Fraaije MW Angew Chem Int Ed Engl. 2016 Nov 22. doi: 10.1002/anie.201608951. PMID:27873437 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monooxygenase 3D structures

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