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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&gt;C (Val110Leu) and 6458A&gt;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. CYP2A6(*)35 (6458A&gt;T) occurred at a frequency of 2.5-2.9% among individuals of black African descent, 0.5-0.8% among Asians and was not found in Caucasians. In addition, we identified two novel alleles, CYP2A6(*)36 (6458A&gt;T and 6558T&gt;C (Ile471Thr)) and CYP2A6(*)37 (6458A&gt;T, 6558T&gt;C and 6600G&gt;T (Arg485Leu)). In vivo, CYP2A6(*)35 was associated with lower CYP2A6 activity as measured by the 3HC/COT ratio. In vitro, CYP2A6.35 had decreased nicotine C-oxidation activity and thermal stability. In conclusion, we identified three novel CYP2A6 alleles (CYP2A6(*)35, (*)36 and (*)37); the higher allele frequency variant CYP2A6(*)35 was associated with lower CYP2A6 activity.

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