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Literature summary for 1.1.1.95 extracted from
- A novel alpha-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12, and its possible implications for human 2-hydroxyglutaric aciduria (1996), J. Bacteriol., 178, 232-239.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression of serA gene, that codes for the enzyme, in Escherichia coli strain JM105 | Escherichia coli |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 3-phosphoglycerate | - |
Escherichia coli |  |
| glycine | - |
Escherichia coli | |
| hydroxyglutarate | product inhibition of the alpha-ketoglutarate reduction | Escherichia coli | |
| L-serine | allosteric inhibition, regulates the pathway of serine biosynthesis by end product inhibition interacting with His344, Asn346 and Asn364 | Escherichia coli | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0032 | - |
3-phosphohydroxypyruvate | apparent | Escherichia coli | |
| 0.088 | - |
alpha-ketoglutarate | apparent | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-phosphoglycerate + NAD+ | Escherichia coli | allosteric inhibition by L-serine, L-serine regulates the pathway of serine biosynthesis by end product inhibition interacting with His344, Asn346 and Asn364, 1 serine binds per subunit | 3-phosphohydroxypyruvate + NADH | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 3-phospho-D-glycerate + NAD+ = 3-phosphooxypyruvate + NADH + H+ | member of the 2-hydroxyacid dehydrogenases family, whereof only the enzymes from E. coli and Pisum sativum utilize phosphorylated substrates and transfer the hydride ion to the A-site of NAD+, uses also alpha-ketoglutarate as substrate | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 8.7 | - |
3-phosphohydroxypyruvate reduction | Escherichia coli |
| 9.7 | - |
alpha-ketoglutarate reduction | Escherichia coli |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -75°C, 15% glycerol, purified stable for months | Escherichia coli |
| 4°C, purified stable for weeks | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-phosphoglycerate + NAD+ | - |
Escherichia coli | 3-phosphohydroxypyruvate + NADH | - |
r | |
| 3-phosphoglycerate + NAD+ | allosteric inhibition by L-serine, L-serine regulates the pathway of serine biosynthesis by end product inhibition interacting with His344, Asn346 and Asn364, 1 serine binds per subunit | Escherichia coli | 3-phosphohydroxypyruvate + NADH | - |
r | |
| alpha-ketoglutarate + NADH | - |
Escherichia coli | 2-hydroxyglutaric acid + NAD+ | both D- and L-isomer serve as substrate for the reverse reaction, but L-isomer is a poor substrate and probably due to contamination | r | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | 50 | reduction, but enzyme is thermally unstable, therefore assay is performed at 37°C | Escherichia coli |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
3 min, 40% loss of reductase activity | Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.463 | - |
3-phosphohydroxypyruvate | apparent | Escherichia coli | |
| 0.555 | - |
alpha-ketoglutarate | apparent | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
3-phosphohydroxypyruvate and alpha-ketoglutarate reduction, enzyme and substrate not stable, product inhibition | Escherichia coli |
| 9.5 | - |
oxidation of D-3-phosphoglycerate | Escherichia coli |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 8.5 | activity drops sharply above pH 8.5 | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | hydride ion is transferred to A-site | Escherichia coli | |
| NADH | - |
Escherichia coli | |
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