Ketone monooxygenases

More recently, Jansen and coworkers [90] used 4-hydroxyacetophenone monooxygenase (HAPMO) for aerobic oxidation of sulfides. Interestingly, both PhSMe and p-MeC6H4SMe gave the corresponding sulfoxides in 99% ee, which should be compared with the 99 and 37% ee, respectively, obtained with CHMO [86]. The flavoenzyme HAPMO, which has been cloned [90, 91], is a promising biocatalyst for enantioselective oxidation of sulfides to sulfoxides. 

Recombinant of baker s yeast expressing CHMO from Actinobactersp. NCIP 9871 have been used as whole-cell biocatalysts for oxidation of sulfides to their corresponding sulfoxides (Eq. (8.20)) [92]. 

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Linear ketone monooxygenase (BVMOpaJ Pseudomonas fluorescens DSM 50106 2006 [42] 2006 [42] [42]... 

Monocyclic monoterpene ketone monooxygenase Rhodococcus erythropolis DCL 14 1 single polypeptide NADPH 60 FAD 9.0 [51]... 

The November 2001 issue of the Journal of Chemical Education ipp 1533-1534) describes an introductory biochemistry laboratory ex periment involving cycio hexanone monooxygenase oxidation of cyclic ketones... 

Although a maj ority of research activities were dedicated to cycloketone converting BVMOs, the recently discovered novel MOs also enable stereoselective oxidation of noncyclic ketones to esters. An aliphatic open-chain monooxygenase (AOCMO) from Pseudomonas Jluorescens DSM 50106 displays stereoselective biooxidation of terminal acyl-groups in proximity to hydroxyls (Scheme 9.23). The biooxidation gives acetic... 

The assessment of clearance is complicated by the numerous mechanisms by which compounds may be cleared from the body. These mechanisms include oxidative metabolism, most commonly by CYP enzymes, but also in some cases by other enzymes including but not limited to monoamine oxidases (MAO), flavin-containing monooxygenases (FMO), and aldehyde oxidase [45, 46], Non-oxidative metabolism such as conjugation or hydrolysis may be effected by enzymes such as glucuronyl transferases (UGT), glutathione transferases (GST), amidases, esterases, or ketone reductases, as well as other enzymes [47, 48], In addition to metabolic pathways, parent compound may be excreted directly via passive or active transport processes, most commonly into the urine or bile. 

Kirschner, A. and Bornscheuer, U.T., Kinetic resolution of 4-hydroxy-2-ketones catalyzed by a Baeyer-Villiger monooxygenase. Angew. Chem. Int. Ed., 2006,45, 7004. 

Geitner, K., Kirschner, A., Rehdorf, J., Schmidt, M., Mihovilovic, M.D. and Bornscheuer, U.T., Enantioselective kinetic resolution of 3-pheny 1-2-ketones using Baeyer-Villiger monooxygenases. Tetrahedron Asymm., 2007,18, 892. 

Rodriguez, C., de Gonzalo, G., Eraaije, M.W. and Gotor, V., Enzymatic kinetic resolution of racemic ketones catalyzed by Baeyer-Villiger monooxygenases. Tetrahedron Asymm., 2007, 18, 1338. 

Baeyer-Villiger reaction Aldehyde, ketones Flavine monooxygenase Esters, lactones... 

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