Cyclohexanone monooxygenase (CHMO) is a flavoprotein that carries out the archetypical Baeyer−Villiger oxidation of a variety of cyclic ketones into lactones. Using NADPH and O2 as cosubstrates, the enzyme inserts one atom of oxygen into the substrate in a complex catalytic mechanism that involves the formation of a flavin-peroxide and Criegee intermediate. We present here the atomic ...

Cyclohexanone monooxygenase (CHMO) uses NADPH and O 2 as cosubstrates and FAD as a cofactor to insert an oxygen atom into the substrate. The process involves the formation of a falvin-peroxide and Criegee intermediate. [7] CHMO is a member of the Baeyer-Villiger monooxygenase (BVMO) family and flavin-containing monooxygenases (FMO) superfamily. [7] ...

2009年3月31日 · Cyclohexanone monooxygenase (CHMO) is a flavoprotein that carries out the archetypical Baeyer-Villiger oxidation of a variety of cyclic ketones into lactones. Using NADPH and O(2) as cosubstrates, the enzyme inserts one atom of oxygen into the substrate in a complex catalytic mechanism that involves the formation of a flavin-peroxide and ...

2016年11月22日 · Cyclohexanone monooxygenase (CHMO; EC 1.14.13.22) is an FAD- and NADPH-dependent Baeyer–Villiger monooxygenase (BVMO). 1 A wide variety of ketones are converted by CHMO into esters or lactones through the insertion of an oxygen atom on one side or the other of the carbonyl group. In addition, CHMO oxidizes aldehydes and heteroatoms 2 and carries out epoxidation reactions. 3 In contrast to ...

2016年10月6日 · Crystal structure of cyclohexanone monooxygenase from Thermocrispum municipale in the oxidised state with a bound nicotinamide. ... Cyclohexanone monooxygenase (CHMO) is a promising biocatalyst for industrial reactions owing to its broad substrate spectrum and excellent regio-, chemo-, and enantioselectivity. ...

2016年10月6日 · 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.

环己酮单加氧酶（CHMO）由于其广泛的底物谱以及出色的区域，化学和对映选择性而成为一种有希望的工业反应生物催化剂。然而，许多Baeyer-Villiger单加氧酶的低稳定性是其在工业中开发的障碍。报道了来自Thermocrispum Municipale的稳健的CHMO的表征和晶体结构测定。

Cyclohexanone monooxygenase (CHMO) is a flavoprotein that carries out the archetypical Baeyer−Villiger oxidation of a variety of cyclic ketones into lactones. Using NADPH and O2 as cosubstrates, the enzyme inserts one atom of oxygen into the substrate in a complex catalytic mechanism that involves the formation of a flavin-peroxide and Criegee intermediate.

2016年12月12日 · Cyclohexanone monooxygenase (CHMO; EC 1.14.13.22) is an FAD‐ and NADPH‐dependent Baeyer–Villiger monooxygenase (BVMO).1 A wide variety of ketones are converted by CHMO into esters or lactones through the insertion of an oxygen atom on one side or the other of the carbonyl group. In addition, CHMO oxidizes aldehydes and heteroatoms2 and carries out epoxidation reactions.3 In contrast to ...

SI 1 Crystal Structures of Cyclohexanone Monooxygenase Reveal Complex Domain Movements and a Sliding Cofactor I. Ahmad Mirza,† Brahm J. Yachnin,† Shaozhao Wang,‡ Stephan Grosse,‡ Hélène Bergeron,‡ Akihiro Imura,|| Hiroaki Iwaki,§ Yoshie Hasegawa,§ Peter C. K. Lau,*,‡ and Albert M. Berghuis*,† Departments of Biochemistry and Microbiology & Immunology, McGill University, 3649 Prom