Studies on the substrate specificity and inducibility of cytochrome P-450meg

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Abstract
The cytochrome P-450-dependent steroid 15.beta.-hydroxylase system in B. megaterium ATCC 13368 was investigated with regard to its appearance in the cell with respect to the growth curve of the organism, with regard to its inducibility by a number of agents (among them some of the classical inducers of the mammalian liver microsomal cytochrome P-450 system) and with regard to its capacity to convert non-steroidal substances into oxygenated compounds. The enzyme reached a maximum concentration in the cell during the stationary phase of the growth curve. Of all agents tested as inducers, none showed any capacity to induce cytochrome P-450meg. Of the substances tested as substrates only aniline (p-hydroxylation) was metabolized by the microbial enzyme system. This conversion might be related to the general oxygenase activity of hemoproteins. The substrate specificity of the .BETA.. megaterium hydroxylase system is apparently narrow.

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