Abstract
A cytochrome P-450-dependent monooxygenase system that catalyzes the stereospecific hydroxylation of the monoterpene substrate 1,4-cineole was demonstrated in cell-free preparations of Bacillus cereus UI-1477. 1,4-Cineole hydroxylations were catalyzed by a 100,000 x g (1-h)-centrifuging soluble, hexane-inducible enzyme that activated and incorporated molecular oxygen into hydroxylated products; required NADH; was inhibited by SKF-525A, imidazole, metyrapone, and octylamine; and displayed a 452-nm peak in the carbon monoxide difference absorption spectrum. The constant 7:1 ratio of endo/exo alcohol products formed when 1,4-cineole was hydroxylated by normal cells, hexane-induced cells, and cell extracts suggested that a single enzyme designated cytochrome P-450cin was responsible for both reactions.
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- Berg A., Carlstrom K., Gustafsson J. A., Ingelman-Sundberg M. Demonstration of a cytochrome P-450-dependent steroid 15beta-hydroxylase in Bacillus megaterium. Biochem Biophys Res Commun. 1975 Oct 27;66(4):1414–1423. doi: 10.1016/0006-291x(75)90517-3. [DOI] [PubMed] [Google Scholar]
- Cardini G., Jurtshuk P. The enzymatic hydroxylation of n-octane by Corynebacterium sp. strain 7E1C. J Biol Chem. 1970 Jun 10;245(11):2789–2796. [PubMed] [Google Scholar]
- Enzymes in organic synthesis. Ciba Found Symp. 1985;111:1–248. [PubMed] [Google Scholar]
- Gunsalus I. C., Sligar S. G. Oxygen reduction by the P450 monoxygenase systems. Adv Enzymol Relat Areas Mol Biol. 1978;47:1–44. doi: 10.1002/9780470122921.ch1. [DOI] [PubMed] [Google Scholar]
- Hare R. S., Fulco A. J. Carbon monoxide and hydroxymercuribenzoate sensitivity of a fatty acid (omega-2) hydroxylase from Bacillus megaterium. Biochem Biophys Res Commun. 1975 Jul 22;65(2):665–672. doi: 10.1016/s0006-291x(75)80198-7. [DOI] [PubMed] [Google Scholar]
- Kim B. H., Fulco A. J. Induction by barbiturates of a cytochrome P-450-dependent fatty acid monooxygenase in Bacillus megaterium: relationship between barbiturate structure and inducer activity. Biochem Biophys Res Commun. 1983 Nov 15;116(3):843–850. doi: 10.1016/s0006-291x(83)80219-8. [DOI] [PubMed] [Google Scholar]
- Narhi L. O., Fulco A. J. Phenobarbital induction of a soluble cytochrome P-450-dependent fatty acid monooxygenase in Bacillus megaterium. J Biol Chem. 1982 Mar 10;257(5):2147–2150. [PubMed] [Google Scholar]
- Riege P., Schunck W. H., Honeck H., Müller H. G. Cytochrome P-450 from Lodderomyces elongisporus: its purification and some properties of the highly purified protein. Biochem Biophys Res Commun. 1981 Jan 30;98(2):527–534. doi: 10.1016/0006-291x(81)90872-x. [DOI] [PubMed] [Google Scholar]
- Rosazza J. P., Steffens J. J., Sariaslani F. S., Goswami A., Beale J. M., Reeg S., Chapman R. Microbial hydroxylation of 1,4-cineole. Appl Environ Microbiol. 1987 Oct;53(10):2482–2486. doi: 10.1128/aem.53.10.2482-2486.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ruettinger R. T., Griffith G. R., Coon M. J. Characterization of the omega-hydroxylase of Pseudomonas oleovorans as a nonheme iron protein. Arch Biochem Biophys. 1977 Oct;183(2):528–537. doi: 10.1016/0003-9861(77)90388-5. [DOI] [PubMed] [Google Scholar]
- Wen L. P., Fulco A. J. Cloning of the gene encoding a catalytically self-sufficient cytochrome P-450 fatty acid monooxygenase induced by barbiturates in Bacillus megaterium and its functional expression and regulation in heterologous (Escherichia coli) and homologous (Bacillus megaterium) hosts. J Biol Chem. 1987 May 15;262(14):6676–6682. [PubMed] [Google Scholar]
- Wen L. P., Fulco A. J. Induction of a cytochrome P-450-dependent fatty acid monooxygenase in Bacillus megaterium by a barbiturate analog, 1-[2-phenylbutyryl]-3-methylurea. Mol Cell Biochem. 1985 May;67(1):77–81. doi: 10.1007/BF00220988. [DOI] [PubMed] [Google Scholar]