Nicotine metabolism by rat hepatic cytochrome P450s.

Article Details

Citation

Copy to clipboard

Nakayama H, Okuda H, Nakashima T, Imaoka S, Funae Y

Nicotine metabolism by rat hepatic cytochrome P450s.

Biochem Pharmacol. 1993 Jun 22;45(12):2554-6.

PubMed ID

8328992 [ View in PubMed

]

Abstract

Many kinds of cytochrome P450s were purified from rat hepatic microsomes, and their role in the metabolization of nicotine in a reconstituted system examined. Of four phenobarbital-inducible P450s, P450 2B1 had the highest nicotine oxidation activity and P450 2B2 showed a low rate of nicotine oxidation, whereas P450 2C6 and 3A2 had no detectable activity toward nicotine. Among eleven other purified cytochrome P450s tested, P450 2C11 had high nicotine oxidation activity and P450 1A2 and 2D1 showed low catalytic activity toward nicotine. The other cytochrome P450s, P450 1A1, 2A1, 2A2, 2C7, 2C12, 2C13, 2E1 and 4A1, had no detectable nicotine oxidation activity. Based on these results, participation of cytochrome P450s in nicotine metabolism in human and animal livers is discussed.

DrugBank Data that Cites this Article

Drug Enzymes

Drug	Enzyme	Kind	Organism	Pharmacological Action	Actions
Nicotine	Cytochrome P450 2E1	Protein	Humans	Unknown	Substrate Inhibitor Inducer	Details