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J. Biol. Chem., Vol. 261, Issue 16, 7160-7169, Jun, 1986
LO Narhi and AJ Fulco
A unique cytochrome P-450-dependent fatty acid monooxygenase from Bacillus
megaterium ATCC 14581 is strongly induced by phenobarbital (Narhi, L. O.,
and Fulco, A. J. (1982) J. Biol. Chem. 257, 2147-2150) and many other
barbiturates (Kim, B.-H., and Fulco, A. J. (1983) Biochem. Biophys. Res.
Commun. 116, 843-850). This monooxygenase has now been purified to
homogeneity from pentobarbital-induced bacteria as a single polypeptide
with a molecular weight of 119,000 +/- 5,000 daltons. In the presence of
NADPH and O2, it can catalyze the oxygenation of long chain fatty acids
without the aid of any other protein. The enzyme has a catalytic center
activity of 4,600 nmol of fatty acid oxygenated per nmol of P-450 (the
highest activity yet reported for a P-450-dependent monooxygenase) and also
functions as a highly active cytochrome c reductase in the presence of
NADPH. The purified holoenzyme is a soluble protein containing 40 mol %
hydrophobic amino acid residues and 1 mol each of FAD and FMN/mol of heme.
It is isolated and purified in the low spin form but is converted to the
high spin form in the presence of long chain fatty acids. The enzyme, which
catalyzes the omega-2 hydroxylation of saturated fatty acids and the
hydroxylation and epoxidation of unsaturated fatty acids has its highest
affinity (Km = 2 +/- 1 microM) for the C15 and C16 chain lengths.
Characterization of a catalytically self-sufficient 119,000-dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium
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