Title : Key residues controlling phenacetin metabolism by human cytochrome P450 2A enzymes.

Pub. Date : 2008 Dec

PMID : 18779312






5 Functional Relationships(s)
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Protein Name
Organism
1 Enzyme kinetics revealed that the CYP2A6 I208S/I300F/G301A/S369G mutant protein O-deethylated phenacetin with a K(m) of 10.3 muM and a k(cat) of 2.9 min(-1), which compare very favorably with those of CYP2A13 (K(m) of 10.7 muM and k(cat) of 3.8 min(-1)). Phenacetin cytochrome P450 family 2 subfamily A member 6 Homo sapiens
2 A 2.15 A crystal structure of the mutant CYP2A6 I208S/I300F/G301A/S369G protein with phenacetin in the active site provided a structural rationale for the differences in phenacetin metabolism between CYP2A6 and CYP2A13. Phenacetin cytochrome P450 family 2 subfamily A member 6 Homo sapiens
3 A 2.15 A crystal structure of the mutant CYP2A6 I208S/I300F/G301A/S369G protein with phenacetin in the active site provided a structural rationale for the differences in phenacetin metabolism between CYP2A6 and CYP2A13. Phenacetin cytochrome P450 family 2 subfamily A member 6 Homo sapiens
4 A 2.15 A crystal structure of the mutant CYP2A6 I208S/I300F/G301A/S369G protein with phenacetin in the active site provided a structural rationale for the differences in phenacetin metabolism between CYP2A6 and CYP2A13. Phenacetin cytochrome P450 family 2 subfamily A member 6 Homo sapiens
5 A 2.15 A crystal structure of the mutant CYP2A6 I208S/I300F/G301A/S369G protein with phenacetin in the active site provided a structural rationale for the differences in phenacetin metabolism between CYP2A6 and CYP2A13. Phenacetin cytochrome P450 family 2 subfamily A member 6 Homo sapiens