Protein Variants | Comment | Organism |
---|---|---|
P268A | 40fold reduction in activity, concentration of N-(phosphonoacetyl)-L-aspartate for maximal activation is increased 233fold as compared to the wild-type, less activation by ATP, stronger inhibition by CTP | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | sigmoidal saturation curve for aspartate | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | - |
Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
carbamoylphosphate + L-aspartate | Escherichia coli | - |
phosphate + N-carbamoyl-L-aspartate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
carbamoyl phosphate + L-aspartate | - |
Escherichia coli | phosphate + N-carbamoyl-L-aspartate | - |
? | |
carbamoylphosphate + L-aspartate | - |
Escherichia coli | phosphate + N-carbamoyl-L-aspartate | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | holoenzyme is a dodecamer composed of 2 catalytic trimers and 3 regulatory dimers, the catalytic chain is composed of 2 structural domains, the aspartate domain and the carbamoylphosphate domain which are involved in the binding of aspartate and carbamoylphosphate respectively, the regulatory chain is also composed of 2 domains, the allosteric and the zinc domains, which are involved in the binding of allosteric effectors and zinc | Escherichia coli |