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

Pub. Date : 2012

PMID : 22382327






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Cytochrome P450 2A6 (CYP2A6) catalyzes important metabolic reactions of many xenobiotic compounds, including coumarin, nicotine, cotinine, and clinical drugs. coumarin cytochrome P450 family 2 subfamily A member 6 Homo sapiens
2 Cytochrome P450 2A6 (CYP2A6) catalyzes important metabolic reactions of many xenobiotic compounds, including coumarin, nicotine, cotinine, and clinical drugs. coumarin cytochrome P450 family 2 subfamily A member 6 Homo sapiens
3 In the case of coumarin 7-hydroxylation, CYP2A6*8 and *35 displayed increased K(m) values whereas CYP2A6*18 and *19 showed decreased k(cat) values, which resulted in lower catalytic efficiencies (k(cat)/K(m)). coumarin cytochrome P450 family 2 subfamily A member 6 Homo sapiens
4 In the case of coumarin 7-hydroxylation, CYP2A6*8 and *35 displayed increased K(m) values whereas CYP2A6*18 and *19 showed decreased k(cat) values, which resulted in lower catalytic efficiencies (k(cat)/K(m)). coumarin cytochrome P450 family 2 subfamily A member 6 Homo sapiens