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- W93963094 abstract "Membrane fractions of benzoate-induced Rhodotorula,graminis hydroxylated benzoate in the para position as demonstrated by high-performance liquid chromatography and isotopic thin-layer chromatography. Benzoate-4-hydroxylase activity was linear as a function of enzyme concentration (washed membranes) and time, and exhibited a pH optimum of 7.6. The enzyme utilized NADPH as a source of reducing equivalents, and was stimulated by FAD. The Km's for benzoate and NADPH were calculated as ∼2.9 × 10−5 M and ∼1.9 × 10−5 M, respectively. The particulate nature of benzoate-4-hydroxylase together with the fact that the enzyme was pteridine-independent indicates that it is distinct from the isofunctional enzyme previously described in filamentous fungi." @default.
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- W93963094 date "1985-06-01" @default.
- W93963094 modified "2023-09-25" @default.
- W93963094 title "Properties of a membrane-associated benzoate-4-hydroxylase from Rhodotorula,graminis" @default.
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- W93963094 doi "https://doi.org/10.1016/0006-291x(85)90177-9" @default.
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