Partial characterization of a barbiturate-induced cytochrome P-450-dependent fatty acid monooxygenase from Bacillus megaterium.
A soluble cytochrome P-450-dependent fatty acid monooxygenase activity obtained from Bacillus megaterium ATCC 14581 can be induced by at least 13 different barbiturates. In general, the potency of these compounds as inducers increases with their increasing lipophilicity. We have now shown that at least 4 of these barbiturates (phenobarbital, secobarbital, pentobarbital and methohexital) seem to induce the same active cytochrome P-450-containing enzyme by a non-substrate type mechanism. The partially purified enzymes obtained from cultures induced with each of the 4 barbiturates tested were all of similar molecular size (Mr = 130,000 +/- 10,000) and had similar turnover numbers (1400-1800 +/- 300) with either palmitoleate or myristate as substrates. None of the tested barbiturates served as substrates, activators or inhibitors of any of the monooxygenase preparations, nor did they appear to interact in any way with the monooxygenase enzyme or the P-450 component.
D001410:Bacillus megaterium / Q000201:enzymology*; D001463:Barbiturates / Q000494:pharmacology*; D003577:Cytochrome P-450 Enzyme System; D004790:Enzyme Induction; D007700:Kinetics; D008723:Methohexital / Q000494:pharmacology; D010105:Oxygenases / Q000235:genetics / Q000302:isolation & purification*; D010424:Pentobarbital / Q000494:pharmacology; D010634:Phenobarbital / Q000494:pharmacology; D012631:Secobarbital / Q000494:pharmacology
D001463:Barbiturates; D012631:Secobarbital; D003577:Cytochrome P-450 Enzyme System; D008723:Methohexital; D010105:Oxygenases; D010424:Pentobarbital; D010634:Phenobarbital