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Literature summary for 2.6.1.1 extracted from
- Glutamate-aspartate transaminase from microorganisms (1985), Methods Enzymol., 113, 83-89.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.01 | - |
oxaloacetate | 25°C, pH 8.0 | Escherichia coli |  |
| 0.24 | - |
2-oxoglutarate | 25°C, pH 8.0 | Escherichia coli | |
| 1.3 | - |
L-aspartate | 25°C, pH 8.0 | Escherichia coli | |
| 15 | - |
L-glutamate | 25°C, pH 8.0 | Escherichia coli | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 43000 | - |
2 * 43000, SDS-PAGE | Escherichia coli |
| 84000 | - |
meniscus depletion sedimentation equilibrium method | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-aspartate + 2-oxoglutarate | Escherichia coli | - |
oxaloacetate + L-glutamate | - |
? | |
| L-aspartate + 2-oxoglutarate | Escherichia coli B / ATCC 11303 | - |
oxaloacetate + L-glutamate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
B | - |
| Escherichia coli | - |
isoenzymes A and B | - |
| Escherichia coli B / ATCC 11303 | - |
B | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| isoenzymes A and B | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Escherichia coli |
| 200 | - |
purified enzyme | Escherichia coli |
| 210 | - |
purified apoenzyme | Escherichia coli |
Storage Stability
| Storage Stability | Organism |
|---|---|
| 4°C, 0.01 M potassium phosphate buffer, pH 7.0, 0.001 mM pyridoxal 5'-phosphate, 75% ammonium sulfate, stable for several months | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-aspartate + 2-oxoglutarate | - |
Escherichia coli | oxaloacetate + L-glutamate | - |
? | |
| L-aspartate + 2-oxoglutarate | - |
Escherichia coli B / ATCC 11303 | oxaloacetate + L-glutamate | - |
? | |
| additional information | substrate specificity | Escherichia coli | ? | - |
? | |
| additional information | substrate specificity | Escherichia coli B / ATCC 11303 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 43000, SDS-PAGE | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | 8.5 | - |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | 2 mol of pyridoxal phosphate per mol of enzyme | Escherichia coli | |
| pyridoxal 5'-phosphate | a pyridoxal 5'-phosphate protein | Escherichia coli | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Escherichia coli | - |
- |
4.2 |
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Release 2023.1 (January 2023)
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