Characteristics of a cytochrome P-450-dependent fatty acid ω-2 hydroxylase from Bacillus megaterium

摘要: Abstract The fatty acid (ω-2) hydroxylase from Bacillus megaterium ATCC 14581 was examined with respect to some general enzymatic properties attributed an intact complex isolated in a partially purified state. Hydroxylase specific activity found increase increasing protein concentration manner consistent reversible association of the components complex. There substantial kinetic lag phase for palmitate hydroxylation which abolished by substrate preincubation absence NADPH. bound and presumably activated without formation substrate-derived intermediate. oxidation NADPH were occur one molar ratio, independent concentration. Finally, cytochrome P -450 component identified on basis its CO-binding difference spectrum. It appears, that this is not identical meg steroid system B. 13368, since progesterone, active latter, hydroxylated preparation 14581.