Effect of acetone on aniline hydroxylation by a reconstituted system.
Acetone stimulated NADPH-dependent aniline hydroxylation catalysed by cytochrome P-450 purified from phenobarbital-treated rats. No activation by acetone occurred in a reconstituted system containing cytochrome P-448 purified from 3-methylcholanthrene-treated rats. Cumene hydroperoxide-supported aniline hydroxylation catalysed by cytochrome P-450 was not increased by the addition of acetone at the concentration which stimulated NADPH-dependent aniline hydroxylation in the reconstituted system. The NADPH-dependent cytochrome P-450 reduction was stimulated by acetone in the presence or absence of aniline. On the other hand, acetone did not exhibit any stimulatory effect on NADPH-dependent reduction of cytochrome P-448. The stimulatory effect of acetone on aniline hydroxylation was decreased with increasing pH of the reaction media. Furthermore, in the system containing cytochrome P-450, the ratio of product to hydrogen peroxide formation was virtually unchanged by the addition of acetone.
D000096:Acetone / Q000494:pharmacology*; D000814:Aniline Compounds / Q000378:metabolism*; D000818:Animals; D019388:Cytochrome P-450 CYP1A2; D003580:Cytochromes / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D006861:Hydrogen Peroxide / Q000096:biosynthesis; D006863:Hydrogen-Ion Concentration; D006900:Hydroxylation; D066298:In Vitro Techniques; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism*; D010084:Oxidation-Reduction; D051381:Rats
D000814:Aniline Compounds; D003580:Cytochromes; D000096:Acetone; D006861:Hydrogen Peroxide; C017170:Cyp1a2 protein, rat; D019388:Cytochrome P-450 CYP1A2; D009251:NADPH-Ferrihemoprotein Reductase; C023650:aniline