• Archives of Pharmacal Research
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• v.15 no.3
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• pp.215-219
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• 1992

S. fradiae exhibited the highest acetanilide p-hydroxylation activity among the Streptomyces spp. screened. Studies with inhibitors (metyrapone, 2. 6-dichloroindophenol, $\alpha,\alpha'$-dipyridyl, o-phenanthroline) and an absorption peak after CO treatment suggested that S. fradiae hydroxylase activity was due to cytochrome p-450. This hydroxylase activity was increased to ten times in the cell extract containing 0.5 mM sodium azide. Furthermore, the sedimentary activity in $105,000\times{g}$ centrifugal forces and solubilization of the activity with Triton-X 100 implied that this enzyme was membrane bound monooxygenase. pH Optimum of the enzyme was 6.5 in membrane bound state.