Protein Variants | Comment | Organism |
---|---|---|
delT236_I242 | either deletion of a 7 amino acid long segment or its replacement by polyproline repeats (5 and 10 residues) results in a significant increase in 2',5'-ADP enthalpy of binding. This is accompanied by a decrease in the number of thermodynamic microstates available for the ligand-cytochrome P450 reductase complex. The estimated heat capacity change for this interaction changes from -220 cal/mol*K in the wild-type enzyme to -580 cal/mol*K in the deletion mutant. Presteady-state kinetics measurements reveal a 50fold decrease in the microscopic rate for interdomain (FAD/FMN) electron transfer in the deletion mutant. Multiple turnover cytochome c reduction assays indicate that these mutations impair the ability of the FMN-binding domain to shuttle electrons from the FAD-binding domain to the cytochrome partner | Homo sapiens |
delT236_I242ins(Pro)10 | either deletion of a 7 amino acid long segment or its replacement by polyproline repeats (5 and 10 residues) results in a significant increase in 2',5'-ADP enthalpy of binding. This is accompanied by a decrease in the number of thermodynamic microstates available for the ligand-cytochrome P450 reductase complex | Homo sapiens |
delT236_I242ins(Pro)5 | either deletion of a 7 amino acid long segment or its replacement by polyproline repeats (5 and 10 residues) results in a significant increase in 2',5'-ADP enthalpy of binding. This is accompanied by a decrease in the number of thermodynamic microstates available for the ligand-cytochrome P450 reductase complex | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
CPR | - |
Homo sapiens |
cytochrome P450 reductase | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Homo sapiens | |
FMN | - |
Homo sapiens |