EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.1.3.2 | X-ray structure of the holoenzyme in the presence of the substrate analog N-phosphonoacetyl-L-aspartate, carbamoylphosphate and succinate | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.1.3.2 | CTP | - |
Escherichia coli | |
2.1.3.2 | UTP | - |
Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.3.2 | carbamoylphosphate + L-aspartate | Escherichia coli | - |
phosphate + N-carbamoyl-L-aspartate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.3.2 | Escherichia coli | - |
- |
- |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.1.3.2 | additional information | - |
specific activity of the catalytic subunit alone is about 50% higher than that of the holoenzyme | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.3.2 | carbamoyl phosphate + L-aspartate | - |
Escherichia coli | phosphate + N-carbamoyl-L-aspartate | - |
? | |
2.1.3.2 | carbamoylphosphate + L-aspartate | - |
Escherichia coli | phosphate + N-carbamoyl-L-aspartate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.1.3.2 | More | model for homotrophic cooperativity | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.1.3.2 | ATP | activates | Escherichia coli |