KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0028 | - |
cyanidin | pH 7.5, 30°C | Vitis vinifera | |
0.111 | - |
NADPH | pH 7.5, 30°C | Vitis vinifera |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Vitis vinifera | Q5FB34 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 cyanidin + 4 NADPH + 4 H+ | - |
Vitis vinifera | (+)-epicatechin + (-)-catechin + 4 NADP+ | - |
? | |
additional information | hyperbolic and rapid-equilibrium ordered mechanism, with NADPH binding first. The most likely mechanism is sequential ordered Bi Uni Uni Bi, with NADPH binding first and NADP+ released last, and internal conversion of the first ternary complex, i.e. that associated with the first hydride transfer, is rate-limiting | Vitis vinifera | ? | - |
? |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Vitis vinifera |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | hyperbolic binding of NADPH and NADP+ to the free enzyme, with a single binding site each and with dissociation constants of 0.046 mM for NADPH and 0.083 for NADP+ | Vitis vinifera | |
NADPH | hyperbolic binding of NADPH and NADP+ to the free enzyme, with a single binding site each and with dissociation constants of 0.046 mM for NADPH and 0.083 for NADP+ | Vitis vinifera |