Pub. Date : 1993 Apr
PMID : 8474022
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Expressed CYP1A1 and CYP1A2 both catalyzed the O-deethylation of phenacetin, although the apparent Km was about 4-fold lower for CYP1A2 (25 vs. 108 microM). | Phenacetin | cytochrome P450 family 1 subfamily A member 2 | Homo sapiens |
| 2 | Expressed CYP1A1 and CYP1A2 both catalyzed the O-deethylation of phenacetin, although the apparent Km was about 4-fold lower for CYP1A2 (25 vs. 108 microM). | Phenacetin | cytochrome P450 family 1 subfamily A member 2 | Homo sapiens |
| 3 | Phenacetin O-deethylation exhibited biphasic kinetics in human liver microsomes, and the apparent Km for the high-affinity component (9 +/- 6 microM) was consistent with the involvement of CYP1A2 in this reaction. | Phenacetin | cytochrome P450 family 1 subfamily A member 2 | Homo sapiens |
| 4 | The prototypic CYP1A xenobiotic inhibitor and substrate probes alpha-naphthoflavone, ellipticine, 7-ethoxycoumarin and 7-ethoxyresorufin all inhibited CYP1A1- and CYP1A2-mediated phenacetin O-deethylation as well as the high-affinity component of human liver phenacetin O-deethylase activity. | Phenacetin | cytochrome P450 family 1 subfamily A member 2 | Homo sapiens |
| 5 | The prototypic CYP1A xenobiotic inhibitor and substrate probes alpha-naphthoflavone, ellipticine, 7-ethoxycoumarin and 7-ethoxyresorufin all inhibited CYP1A1- and CYP1A2-mediated phenacetin O-deethylation as well as the high-affinity component of human liver phenacetin O-deethylase activity. | Phenacetin | cytochrome P450 family 1 subfamily A member 2 | Homo sapiens |
| 6 | In contrast, the monoclonal antibody MAb 1-7-1, raised against 3-methylcholanthrene-inducible rat cytochromes 450, almost abolished CYP1A1-mediated phenacetin O-deethylation, but had no effect on human liver microsomal- or CYP1A2-catalyzed phenacetin dealkylation. | Phenacetin | cytochrome P450 family 1 subfamily A member 2 | Homo sapiens |