Pub. Date : 2009
PMID : 20408502
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | The three-dimensional structures of these CYP2F enzymes have been compared by molecular overlay, especially with regard to the active site regions, and it would appear that the substitution of a lysine (Lys-301) in human CYP2F1 for the usual glutamate (Glu-301) in mouse CYP2F2, goat CYPF3 and rat CYP2F4 prior to the conserved distal threonine residue may well constitute a significant factor in any species differences between these CYP2F enzymes. | Lysine | cytochrome P450 family 2 subfamily F member 1 | Homo sapiens |
| 2 | The three-dimensional structures of these CYP2F enzymes have been compared by molecular overlay, especially with regard to the active site regions, and it would appear that the substitution of a lysine (Lys-301) in human CYP2F1 for the usual glutamate (Glu-301) in mouse CYP2F2, goat CYPF3 and rat CYP2F4 prior to the conserved distal threonine residue may well constitute a significant factor in any species differences between these CYP2F enzymes. | Lysine | cytochrome P450 family 2 subfamily F member 1 | Homo sapiens |
| 3 | The three-dimensional structures of these CYP2F enzymes have been compared by molecular overlay, especially with regard to the active site regions, and it would appear that the substitution of a lysine (Lys-301) in human CYP2F1 for the usual glutamate (Glu-301) in mouse CYP2F2, goat CYPF3 and rat CYP2F4 prior to the conserved distal threonine residue may well constitute a significant factor in any species differences between these CYP2F enzymes. | Lysine | cytochrome P450 family 2 subfamily F member 1 | Homo sapiens |
| 4 | The three-dimensional structures of these CYP2F enzymes have been compared by molecular overlay, especially with regard to the active site regions, and it would appear that the substitution of a lysine (Lys-301) in human CYP2F1 for the usual glutamate (Glu-301) in mouse CYP2F2, goat CYPF3 and rat CYP2F4 prior to the conserved distal threonine residue may well constitute a significant factor in any species differences between these CYP2F enzymes. | Lysine | cytochrome P450 family 2 subfamily F member 1 | Homo sapiens |
| 5 | The three-dimensional structures of these CYP2F enzymes have been compared by molecular overlay, especially with regard to the active site regions, and it would appear that the substitution of a lysine (Lys-301) in human CYP2F1 for the usual glutamate (Glu-301) in mouse CYP2F2, goat CYPF3 and rat CYP2F4 prior to the conserved distal threonine residue may well constitute a significant factor in any species differences between these CYP2F enzymes. | Lysine | cytochrome P450 family 2 subfamily F member 1 | Homo sapiens |
| 6 | The three-dimensional structures of these CYP2F enzymes have been compared by molecular overlay, especially with regard to the active site regions, and it would appear that the substitution of a lysine (Lys-301) in human CYP2F1 for the usual glutamate (Glu-301) in mouse CYP2F2, goat CYPF3 and rat CYP2F4 prior to the conserved distal threonine residue may well constitute a significant factor in any species differences between these CYP2F enzymes. | Lysine | cytochrome P450 family 2 subfamily F member 1 | Homo sapiens |