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PMID: 3748010 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Oxidation of quinidine by human liver cytochrome P-450.

Molecular pharmacology ·Vol. 30 ·No. 3 ·1986-09-00 ·Pages 287-95

Guengerich FP, Müller-Enoch D, Blair IA

Abstract

The anti-arrhythmic quinidine has been reported to be a competitive inhibitor of the catalytic activities of human liver P-450DB, including sparteine delta 2-oxidation and bufuralol 1'-hydroxylation, and we confirmed the observation that submicromolar concentrations are strongly inhibitory. Human liver microsomes oxidize quinidine to the 3-hydroxy (Km 4 microM) and N-oxide (Km 33 microM) products, consonant with in vivo observations. Both bufuralol and sparteine inhibited microsomal quinidine 3-hydroxylation. Liver microsomes prepared from DA strain rats showed a relative deficiency in quinidine 3-hydroxylase activity in females compared to males. These observations might suggest that quinidine oxidation is catalyzed by the same P-450 forms that oxidize debrisoquine, bufuralol, and sparteine; i.e., rat P-450UT-H and P-450DB. However, neither of these two purified enzymes catalyzed quinidine 3-hydroxylation, and anti-P-450UT-H, which strongly inhibits human liver microsomal bufuralol 1'-hydroxylation, did not substantially inhibit quinidine 3-hydroxylation or N-oxygenation. P-450MP, the human S-mephenytoin 4-hydroxylase, also does not appear to oxidize quinidine but P-450NF, the human nifedipine oxidase, does. Anti-P-450NF inhibited greater than 95% of the 3-hydroxylation and greater than 85% of the N-oxygenation of quinidine in several microsomal samples. Quinidine inhibited microsomal nifedipine oxidation and, in a series of human liver samples, rates of nifedipine oxidation were correlated with rates of quinidine oxidation. Thus, quinidine oxidation appears to be catalyzed primarily by P-450NF and not by P-450DB. Quinidine binds 2 orders of magnitude more tightly to P-450DB, which does not oxidize it, than to P-450NF, the major enzyme involved in its oxidation. The substrate specificity of human P-450NF is discussed further in terms of its regioselective oxidations of complex molecules including quinidine, aldrin, benzphetamine, cortisol, testosterone and androstenedione, estradiol, and several 2,6-dimethyl-1,4-dihydropyridines.

MeSH Terms
Animals Cytochrome P-450 CYP3A Cytochrome P-450 Enzyme System/pharmacology Ethanolamines/metabolism Humans Hydroxylation In Vitro Techniques Microsomes, Liver/metabolism Nifedipine/metabolism Oxidation-Reduction Quinidine/metabolism,pharmacology Rats
Chemicals
Ethanolamines bufuralol Cytochrome P-450 Enzyme System CYP3A protein, human Cytochrome P-450 CYP3A Nifedipine Quinidine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Guengerich F P
Müller-Enoch D
Blair I A
Article Info
Journal
Molecular pharmacology
Abbr.
Mol Pharmacol
ISSN
0026-895X
Published
1986-09-00
Pages
287-95
Language
English
Region
United States
NLM ID
0035623
Subset
IM
Grants
NCI NIH HHS · CA 30907 · United States
NIEHS NIH HHS · ES 00267 · United States
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