Cyclohexanone monooxygenase (CHMO)

Cyclohexanone monooxygenase (CHMO) is a prototypical bacterial flavoenzyme belonging to the Baeyer-Villiger monooxygenase (BVMO) family. It catalyzes the NADPH-dependent insertion of an oxygen atom into cyclic ketones, such as the conversion of cyclohexanone to epsilon-caprolactone, via a unique peroxyflavin intermediate [1, 4, 25]. While not a direct therapeutic target in humans, CHMO is highly valued in the pharmaceutical industry as a biocatalyst for the enantioselective synthesis of chiral drugs, including the proton pump inhibitor (S)-omeprazole [1, 11, 20]. Furthermore, CHMO serves as a critical structural and mechanistic model for related BVMOs in pathogens like Mycobacterium tuberculosis, where enzymes such as EthA are essential for the bioactivation of anti-tuberculosis prodrugs like ethionamide [2, 3]. Understanding CHMO's function and stability is therefore vital for both green chemistry applications and the development of treatments for drug-resistant bacterial infections [6, 7].

Other names

Baeyer-Villiger monooxygenaseBVMOCyclohexanone 1,2-monooxygenaseCyclohexanone oxygenaseCyclohexanone,NADPH:oxygen oxidoreductase (lactone-forming)

Bioactivation of prodrugs (in pathogens); Biocatalytic synthesis of chiral pharmaceuticals (industrial)