Protein Variants | Comment | Organism |
---|---|---|
E301A | site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview | Anabaena sp. |
additional information | construction of active site mutants | Anabaena sp. |
R100A | site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview | Anabaena sp. |
Y303F | site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview | Anabaena sp. |
Y303S | site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview | Anabaena sp. |
Y303W | site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview | Anabaena sp. |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Stopped-flow pre-steady-state kinetics, overview | Anabaena sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 reduced ferredoxin + NADP+ | Anabaena sp. | - |
2 oxidized ferredoxin + NADPH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Anabaena sp. | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 reduced ferredoxin + NADP+ | - |
Anabaena sp. | 2 oxidized ferredoxin + NADPH + H+ | - |
r | |
2 reduced ferredoxin + NADP+ | two transient charge-transfer complexes occur prior and upon hydride transfer in the reversible reaction, spectral properties and activities of wild-type and mutant enzymes, overview. Need for an adequate initial interaction between the 2'P-AMP portion of NADP+/H and FNR that provides subsequent conformational changes leading to charge-transfer complex formation | Anabaena sp. | 2 oxidized ferredoxin + NADPH + H+ | - |
r |
Synonyms | Comment | Organism |
---|---|---|
adrenodoxin reductase | - |
Anabaena sp. |
FNR | - |
Anabaena sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Anabaena sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Anabaena sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | dependent on | Anabaena sp. |
General Information | Comment | Organism |
---|---|---|
additional information | while in the wild-type, vibrational enhanced modulation of the active site contributes to the tunnel probability of hydride transfer, complexes of some of the active site mutants with the coenzyme hardly allow the relative movement of isoalloxazine and nicotinamide rings along the hydride transfer reaction. The architecture of the wild-type FNR active site precisely contributes to reduce the stacking probability between the isoalloxazine and nicotinamide rings in the catalytically competent complex, modulating the angle and distance between the N5 of the FAD isoalloxazine and the C4 of the coenzyme nicotinamide to values that ensure efficient hydride transfer processes | Anabaena sp. |