5M10

Crystal structure of cyclohexanone monooxygenase from Thermocrispum municipale in the oxidised state with a bound nicotinamide.

5M10 の概要

• エントリーDOI: 10.2210/pdb5m10/pdb
• 分子名称: Cyclohexanone Monooxygenase from Thermocrispum municipale, FLAVIN-ADENINE DINUCLEOTIDE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (7 entities in total)
• 機能のキーワード: cyclohexanone monooxygenase baeyer-villiger monooxygenases flavoenzymes, oxidoreductase
• 由来する生物種: Thermocrispum municipale
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 62551.01

構造登録者

Gomez-Castellanos, J.R.,Mattevi, A. (登録日: 2016-10-06, 公開日: 2016-12-07, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.22 Å)