EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.18.1.2 | additional information | addition of an artificial metal binding site of nine amino acids, including four His residues, to the C-terminal Tyr308 residue. The additional structure binds Zn2+ or Co2+ and significantly reduces the catalytic efficiency of the enzyme by decreasing the kcat value. In absence of Zn2+, Km value of NADPH and Kd value for NADP+ are increased 2 to 3 times | Pisum sativum |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.18.1.2 | 0.0012 | - |
NADPH | wild-type, 30°C, pH 8.0 | Pisum sativum | |
1.18.1.2 | 0.0024 | - |
NADPH | mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, absence of Zn2+, 30°C, pH 8.0 | Pisum sativum | |
1.18.1.2 | 0.0026 | - |
NADPH | mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, presence of Zn2+, 30°C, pH 8.0 | Pisum sativum |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.18.1.2 | Pisum sativum | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.18.1.2 | NADPH + H+ + oxidized 2,6-dichlorophenolindophenol | - |
Pisum sativum | NADP+ + reduced 2,6-dichlorophenolindophenol | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.18.1.2 | 2.2 | - |
NADPH | wild-type, 30°C, pH 8.0 | Pisum sativum | |
1.18.1.2 | 10.1 | - |
NADPH | mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, presence of Zn2+, 30°C, pH 8.0 | Pisum sativum | |
1.18.1.2 | 73.5 | - |
NADPH | mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, absence of Zn2+, 30°C, pH 8.0 | Pisum sativum | |
1.18.1.2 | 74.1 | - |
NADPH | wild-type, 30°C, pH 8.0 | Pisum sativum |