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Literature summary for 1.6.2.4 extracted from

  • Grunau, A.; Geraki, K.; Grossmann, J.G.; Gutierrez, A.
    Conformational dynamics and the energetics of protein-ligand interactions: role of interdomain loop in human cytochrome P450 reductase (2007), Biochemistry, 46, 8244-8255.
    View publication on PubMed

Protein Variants

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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Synonyms

Synonyms Comment Organism
CPR
-
Homo sapiens
cytochrome P450 reductase
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD
-
Homo sapiens
FMN
-
Homo sapiens