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Literature summary for 6.3.4.4 extracted from
- Identification of a essential second metal ion in the reaction mechanism of Escherichia coli adenylosuccinate synthetase (1995), J. Biol. Chem., 270, 15539-15544.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | effect of metal ions on Km-values | Escherichia coli |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | can replace Mg2+ with lower efficiency | Escherichia coli |  |
| Mg2+ | two Mg2+ ions are required. The first metal ion is coordinated with beta-phosphoryl groups and gamma-phosphoryl groups of GTP to provide an electron sink, and the second one seems to interact with Asp in the enzyme active site. Km for Mg2+: 0.114 mM | Escherichia coli | |
| Mn2+ | can replace Mg2+ with lower efficiency | Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GTP + IMP + L-Asp | - |
Escherichia coli | GDP + phosphate + adenylosuccinate | - |
? | |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | - |
Escherichia coli |
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