Purification and characterization of cyclohexanone 1,2-monooxygenase from Exophiala jeanselmei strain KUFI-6N.
Baeyer-Villiger cyclohexanone 1,2-monooxygenase (CHMO) was purified 17.1-fold from cell extracts of the fungus Exophiala jeanselmei grown on cyclohexanol to electrophoretically homogeneity by serial chromatographies. The molecular mass of the native enzyme was approximately 74 kDa by gel filtration and SDS-PAGE. Some enzymic characterizations were studied. The NH2-terminal amino acid residues were Ala-Lys-Ser-Leu-Asp-Val-Leu-Ile-Val-Gly-Ala-Gly-Phe-Gly-Gly-Ile-Tyr-Gln-Leu-, with similarity to the bacterial CHMOs of FAD-binding and NADPH-dependent type Baeyer-Villiger monooxygenases.
Hasegawa
Y
Y
Department of Biotechnology, Faculty of Engineering and High Technology Research Center, Kansai University, Suita, Japan.
Nakai
Y
Y
Tokuyama
T
T
Iwaki
H
H
D000595:Amino Acid Sequence; D003512:Cyclohexanones / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005093:Exophiala / Q000201:enzymology*; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009249:NADP / Q000378:metabolism; D010105:Oxygenases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism*; D011796:Quinacrine / Q000494:pharmacology; D011803:Quinine / Q000494:pharmacology; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D003512:Cyclohexanones; D004791:Enzyme Inhibitors; D005182:Flavin-Adenine Dinucleotide; D009249:NADP; C036468:cyclohexanone; D011803:Quinine; D010105:Oxygenases; C019961:cyclohexanone oxygenase; D011796:Quinacrine