Steroid 9α-hydroxylase is an enzyme found in nocardioform microorganisms which can utilize steroids as a sole carbon source. After fractional centrifugation of the cell homogenates, the enzyme activity inNocardia andRhodococcus was found in cytoplasmic membrane fraction. On the contrary,Mycobacterium had its 9α-hydroxylation activity in cytosolic fraction. To characterize the enzyme in these microorganisms, several potential inhibitors of 9α-hydroxylase were tested and the cofactor requirement for the same enzyme was also examined. The inhibitory effect of ferrous ion chelators indicated involvement of iron containing proteins in the 9α-hydroxylase system. On the other hand, metyrapone, an inhibitor known to be specific for cytochrome P450 interfered with the enzyme inMycobacterium, but didn’t inhibit the enzyme activity inNocardia andRhodococcus. While the 9α-hydroxylase system inNocardia andRhodococcus required NADPH, NADH was required as an election donor inMycobacterium.
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Kang, H.K., Lee, S.S. Heterogeneous natures of the microbial steroid 9α-hydroxylase in nocardioforms. Arch. Pharm. Res. 20, 519–524 (1997). https://doi.org/10.1007/BF02975204
- Steroid 9α-hydroxylase
- Iron-containing protein
- Cytochrome P450