5M10
Crystal structure of cyclohexanone monooxygenase from Thermocrispum municipale in the oxidised state with a bound nicotinamide.
Summary for 5M10
| Entry DOI | 10.2210/pdb5m10/pdb |
| Descriptor | Cyclohexanone Monooxygenase from Thermocrispum municipale, FLAVIN-ADENINE DINUCLEOTIDE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (7 entities in total) |
| Functional Keywords | cyclohexanone monooxygenase baeyer-villiger monooxygenases flavoenzymes, oxidoreductase |
| Biological source | Thermocrispum municipale |
| Total number of polymer chains | 1 |
| Total formula weight | 62551.01 |
| Authors | Gomez-Castellanos, J.R.,Mattevi, A. (deposition date: 2016-10-06, release date: 2016-12-07, Last modification date: 2024-05-08) |
| Primary citation | Romero, E.,Castellanos, J.R.,Mattevi, A.,Fraaije, M.W. Characterization and Crystal Structure of a Robust Cyclohexanone Monooxygenase. Angew. Chem. Int. Ed. Engl., 55:15852-15855, 2016 Cited by PubMed Abstract: 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. PubMed: 27873437DOI: 10.1002/anie.201608951 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.22 Å) |
Structure validation
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