5M0Z

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

Summary for 5M0Z

• Entry DOI: 10.2210/pdb5m0z/pdb
• Descriptor: Cyclohexanone Monooxygenase from Thermocrispum municipale., FLAVIN-ADENINE DINUCLEOTIDE, [(2R,3R,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3-HYDROXY-4-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]METHYL [(2R,3S,4S)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL]METHYL DIHYDROGEN DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: baeyer-villiger monooxygenases flavoenzymes, oxidoreductase
• Biological source: Thermocrispum municipale DSM 44069
• Total number of polymer chains: 1
• Total formula weight: 61788.21

Authors

Gomez-Castellanos, J.R.,Mattevi, A. (deposition date: 2016-10-06, release date: 2016-12-07, Last modification date: 2024-01-17)

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

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: 27873437
DOI: 10.1002/anie.201608951

Experimental method

X-RAY DIFFRACTION (1.6 Å)