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Literature summary for 1.2.1.41 extracted from
- The biosynthesis of proline in Escherichia coli: phosphate-dependent glutamate-semialdehyde dehydrogenase (NADP), the second enzyme in the pathway (1971), Biochim. Biophys. Acta, 244, 129-134.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.18 | - |
NADP+ | - |
Escherichia coli |  |
| 2.2 | - |
glutamic gamma-semialdehyde | - |
Escherichia coli | |
| 11 | - |
phosphate | - |
Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Escherichia coli 55-I | - |
- |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.0072 | - |
crude extract | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-glutamate 5-semialdehyde + phosphate + NADP+ | arsenate can replace phosphate | Escherichia coli | L-5-glutamyl phosphate + NADPH | - |
r | |
| L-glutamate 5-semialdehyde + phosphate + NADP+ | arsenate can replace phosphate | Escherichia coli 55-I | L-5-glutamyl phosphate + NADPH | - |
r | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
- |
Escherichia coli |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.3 | 7.8 | about 30% of activity maximum at pH 7.3, about 20% of activity maximum at pH 7.8 | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADPH | - |
Escherichia coli | |
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Release 2023.1 (January 2023)
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