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Article

Functional characterization of allelic variants of polymorphic human cytochrome P450 2A6 (CYP2A65, 7, 8, 18, 19, and 35).

Biological & pharmaceutical bulletin - 1 Jan 2012

Han Songhee, Choi Seunghye, Chun Young-Jin, Yun Chul-Ho, Lee Chang Hoon, Shin Hee Jung, Na Han Sung, Chung Myeon Woo, Kim Donghak

Abstract excerpt

Cytochrome P450 2A6 (CYP2A6) catalyzes important metabolic reactions of many xenobiotic compounds, including coumarin, nicotine, cotinine, and clinical drugs. Genetic polymorphisms of CYP2A6 can influence its metabolic activities. This study analyzed the functional activities of six CYP2A6 allelic variants (CYP2A6*5, *7, *8, *18, *19, and *35) containing nonsynonymous single-nucleotide polymorphisms. Recombinant...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 22382327
DOI: 10.1248/bpb.35.394

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Functional characterization of allelic variants of polymorphic human cytochrome P450 2A6 (CYP2A6*5, *7, *8, *18, *19, and *35).PMID 22382327Read ↗

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