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Literature summary for 2.1.3.2 extracted from
- Picosecond dynamics of T and R forms of aspartate transcarbamylase: A neutron scattering study (2006), Biochim. Biophys. Acta, 1764, 1527-1535.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | the allosteric enzyme shows homotropic cooperative interactions between the catalytic sites for the binding of aspartate, neuron scattering, protein dynamics, overview | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| carbamoyl phosphate + L-aspartate | Escherichia coli | the enzyme catalyzes the first committed step in pyrimidine biosynthesis | phosphate + N-carbamoyl-L-aspartate | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| carbamoyl phosphate + L-aspartate | the enzyme catalyzes the first committed step in pyrimidine biosynthesis | Escherichia coli | phosphate + N-carbamoyl-L-aspartate | - |
? | |
| carbamoyl phosphate + L-aspartate | substrate binding causes significant conformational changes | Escherichia coli | phosphate + N-carbamoyl-L-aspartate | - |
? | |
| additional information | the allosteric enzyme shows homotropic cooperative interactions between the catalytic sites for the binding of aspartate due to a quarternary structure transition between high aspartate affinity T state and R state | Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | quarternary structure and substrate binding-mediated conformational changes analyzed by inelastic neuron scattering using bisubstrate analogue N-(phosphonacetyl)-L-aspartate binding, protein dynamics, overview | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| aspartate transcarbamylase | - |
Escherichia coli |
| ATCase | - |
Escherichia coli |
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