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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
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 | 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 | Comment | Organism |
---|---|---|
aspartate transcarbamylase | - |
Escherichia coli |
ATCase | - |
Escherichia coli |