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Literature summary extracted from
- The mechanism of end product inhibition of serine biosynthesis. I. purification and kinetics of phosphoglycerate dehydrogenase (1968), J. Biol. Chem., 243, 2081-2089.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.1.1.95 | - |
Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.95 | amino acids | - |
Escherichia coli |  |
| 1.1.1.95 | iodoacetate | - |
Escherichia coli | |
| 1.1.1.95 | L-alanine | - |
Escherichia coli | |
| 1.1.1.95 | L-allothreonine | - |
Escherichia coli | |
| 1.1.1.95 | L-homoserine | - |
Escherichia coli | |
| 1.1.1.95 | L-serine | 50% inhibition at 0.005 mM and pH 7.5 | Escherichia coli | |
| 1.1.1.95 | L-threonine | - |
Escherichia coli | |
| 1.1.1.95 | N-ethylmaleimide | - |
Escherichia coli | |
| 1.1.1.95 | NADH | inhibition of phosphoglycerate oxidation | Escherichia coli | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.95 | 0.008 | - |
NAD+ | - |
Escherichia coli | |
| 1.1.1.95 | 1.1 | - |
D-3-phosphoglycerate | Km at pH 7.5 is lower than at pH 8.8 | Escherichia coli | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.95 | 165000 | - |
gel filtration | Escherichia coli |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.1.95 | Escherichia coli | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.1.1.95 | - |
Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.95 | 3-phospho-D-glycerate + NAD+ | - |
Escherichia coli | 3-phosphohydroxypyruvate + NADH | - |
? | |
| 1.1.1.95 | 3-phosphoglycerate + NAD+ | reduction of hydroxypyruvate-phosphate is faster than oxidation of phosphoglycerate | Escherichia coli | 3-phosphohydroxypyruvate + NADH | - |
r | |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.95 | 25 | - |
assay at | Escherichia coli |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.95 | additional information | - |
additional information | - |
Escherichia coli |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.95 | 8.5 | - |
initial rate maximum, but enzyme not stable | Escherichia coli |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.95 | 5.5 | 8.5 | Tris buffer and phosphate buffer | Escherichia coli |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.95 | 5.5 | 7.5 | stable | Escherichia coli |
| 1.1.1.95 | 8.5 | 9.5 | unstable | Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.95 | 3-acetylpyridine-NADH | 40% as effective as NADH | Escherichia coli | |
| 1.1.1.95 | NAD+ | - |
Escherichia coli | |
| 1.1.1.95 | NADH | - |
Escherichia coli | |
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Release 2023.1 (January 2023)
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