Pub. Date : 1997 Jun
PMID : 9241661
9 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | With cyclophosphamide as substrate, CYP2C19 had the lowest apparent Km, followed by CYP2C9, CYP2C18 and CYP2C8, whereas in the case of ifosfamide, the rank order was: Km CYP2C19 < CYP2C18 < CYP2C9 < CYP2C8. | Cyclophosphamide | cytochrome P450 family 2 subfamily C member 18 | Homo sapiens |
| 2 | With cyclophosphamide as substrate, CYP2C19 had the lowest apparent Km, followed by CYP2C9, CYP2C18 and CYP2C8, whereas in the case of ifosfamide, the rank order was: Km CYP2C19 < CYP2C18 < CYP2C9 < CYP2C8. | Cyclophosphamide | cytochrome P450 family 2 subfamily C member 18 | Homo sapiens |
| 3 | With cyclophosphamide as substrate, CYP2C19 had the lowest apparent Km, followed by CYP2C9, CYP2C18 and CYP2C8, whereas in the case of ifosfamide, the rank order was: Km CYP2C19 < CYP2C18 < CYP2C9 < CYP2C8. | Ifosfamide | cytochrome P450 family 2 subfamily C member 18 | Homo sapiens |
| 4 | CYP2C18 had the highest in vitro intrinsic clearance/catalytic efficiency (apparent Vmax/Km) in cyclophosphamide and ifosfamide activation, followed by 2C19 > 2C9 approximately 2C8. | Cyclophosphamide | cytochrome P450 family 2 subfamily C member 18 | Homo sapiens |
| 5 | CYP2C18 had the highest in vitro intrinsic clearance/catalytic efficiency (apparent Vmax/Km) in cyclophosphamide and ifosfamide activation, followed by 2C19 > 2C9 approximately 2C8. | Ifosfamide | cytochrome P450 family 2 subfamily C member 18 | Homo sapiens |
| 6 | Examination of a panel of CYP2C allelic variants revealed that CYP2C18-Thr385 had both a higher Vmax and a higher apparent Km toward cyclophosphamide than CYP2C18-Met385 with no difference in catalytic efficiency, whereas with ifosfamide the Thr385 allele exhibited a strikingly lower apparent Km resulting in a six-fold higher catalytic efficiency. | Cyclophosphamide | cytochrome P450 family 2 subfamily C member 18 | Homo sapiens |
| 7 | Examination of a panel of CYP2C allelic variants revealed that CYP2C18-Thr385 had both a higher Vmax and a higher apparent Km toward cyclophosphamide than CYP2C18-Met385 with no difference in catalytic efficiency, whereas with ifosfamide the Thr385 allele exhibited a strikingly lower apparent Km resulting in a six-fold higher catalytic efficiency. | Ifosfamide | cytochrome P450 family 2 subfamily C member 18 | Homo sapiens |
| 8 | Thus (a) wild type CYP2C19 and CYP2C9 are relatively low Km catalysts of cyclophosphamide and ifosfamide activation, and (b) all four human CYP2C enzymes activate these two anticancer prodrugs with varying efficiencies and with striking differences among naturally occurring allelic variants in the case of CYP2C9 and CYP2C18. | Cyclophosphamide | cytochrome P450 family 2 subfamily C member 18 | Homo sapiens |
| 9 | Thus (a) wild type CYP2C19 and CYP2C9 are relatively low Km catalysts of cyclophosphamide and ifosfamide activation, and (b) all four human CYP2C enzymes activate these two anticancer prodrugs with varying efficiencies and with striking differences among naturally occurring allelic variants in the case of CYP2C9 and CYP2C18. | Ifosfamide | cytochrome P450 family 2 subfamily C member 18 | Homo sapiens |