PMID: 6990989Jan 1, 1980Paper

Benzo(a)pyrene hydroxylase from Saccharomyces cerevisiae. Substrate binding, spectral and kinetic data

Biochimica Et Biophysica Acta
L F Woods, A Wiseman

Abstract

Saccharomyces cerevisiae, brewer's yeast, produces a microsomal benzo(a)pyrene hydroxylase when grown at high glucose concentrations of which the haemoprotein, cytochrome P-450 (RH, reduced-flavoprotein:oxygen oxidoreductase (RH-hydroxylating) EC 1.14.14.1) is a component. We report here kinetic data derived from Lineweaver-Burk plots of benzo(a)pyrene hydroxylation. The Michaelis constant was decreased by growth of the yeast in the presence of benzo(a)pyrene showing the induction of a form of the enzyme more specific for this compound. NADPH or cumene hydroperoxide could be used as cofactors by this enzyme, although with different Km and V values for benzo(a)pyrene. A solubilised and a solubilised, immobilised enzyme preparation were capable of benzo(a)pyrene hydroxylation, using cumene hydroperoxide but not NADPH as the cofactor. Benzo(a)pyrene was found to produce a modified type I spectral change with yeast and rat liver microsomes. The interaction of benzo(a)pyrene with cytochrome P-450 was investigated further by means of an equilibrium gel filtration technique. There appeared to be 20 binding sites per mol ofcytochrome P-450 for benz(a)pyrene, in both yeast and rat liver microsomes.

References

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Citations

Jan 1, 1983·Molecular & General Genetics : MGG·D J KingD Wilkie
Jan 1, 1992·Journal of Industrial Microbiology·J B Sutherland
Oct 1, 1989·Xenobiotica; the Fate of Foreign Compounds in Biological Systems·D W NebertR Feyereisen
Jul 15, 1983·Archives of Biochemistry and Biophysics·D E Matthews, H D Van Etten
Dec 1, 1984·Xenobiotica; the Fate of Foreign Compounds in Biological Systems·M Kapoor, W S Lin

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