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Article

A novel CYP2A6 allele (CYP2A6*35) resulting in an amino-acid substitution (Asn438Tyr) is associated with lower CYP2A6 activity in vivo.

The pharmacogenomics journal - 1 Aug 2009

Al Koudsi Nael, Ahluwalia Jasjit S, Lin Shih-Ku, Sellers Edward M, Tyndale Rachel F

Abstract excerpt

Cytochrome P450 2A6 (CYP2A6) is the primary human enzyme involved in nicotine metabolism. The objective of this study was to characterize two nonsynonymous single nucleotide polymorphisms in CYP2A6(*)24, 594G>C (Val110Leu) and 6458A>T (Asn438Tyr). We determined their haplotype, allele frequencies, effect on CYP2A6 activity in vivo, as well as their stability and ability to metabolize nicotine in vitro....

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 19365400
DOI: 10.1038/tpj.2009.11
PMCID: PMC2922203

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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