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- W1973182797 abstract "Cytochrome P450 BM-3 fromBacillus megateriumcatalyzes the subterminal hydroxylation of medium- and long-chain fatty acids at the positions ω-1, ω-2, and ω-3. A rapid and continuous spectrophotometric activity assay for cytochrome P450 BM-3 based on the conversion ofp-nitrophenoxycarboxylic acids (pNCA) to ω-oxycarboxylic acids and the chromophorep-nitrophenolate was developed. In contrast to the commonly used activity assays for this enzyme, relying on the consumption of oxygen or NADPH or the use of14C-labeled carboxylic acids, the pNCA assay can even be used with crude extracts of the recombinant enzyme from lysedEscherichia colicells. The kinetics ofp-nitrophenolate formation are directly measured at a wavelength of 410 nm using a spectrophotometer or microtiter plate reader. Sensitivity of the assay is greatly enhanced ifp-nitrophenoxydodecanoic orp-nitrophenoxypentadecanoic acid are used with the F87A mutant instead of the wild-type P450 BM-3 enzyme." @default.
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- W1973182797 date "1989-04-01" @default.
- W1973182797 modified "2023-10-17" @default.
- W1973182797 title "Fluorometric assay of hepatic microsomal monooxygenases by use of 7-methoxyquinoline" @default.
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- W1973182797 doi "https://doi.org/10.1016/0006-2952(89)90346-8" @default.
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