| Autor: |
HASEGAWA, Yoshie, NAKAI, Yuka, TOKUYAMA, Tai, IWAKI, Hiroaki |
| Zdroj: |
Bioscience, Biotechnology, and Biochemistry; January 2000, Vol. 64 Issue: 12 p2696-2698, 3p |
| Abstrakt: |
Baeyer-Villiger cyclohexanone 1,2-monooxygenase (CHMO) was purified 17.1-fold from cell extracts of the fungus Exophiala jeanselmeigrown 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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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