Pub. Date : 2008 Dec
PMID : 18779312
5 Functional Relationships(s)Download |
Sentence | Compound Name | 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 |