Protein Variants | Comment | Organism |
---|---|---|
D236A | the small-angle x-ray scattering pattern of unliganded D236A ATCase differs from the scattering pattern of the wild-type enzyme | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
carbamoyl phosphate + L-aspartate | upon substrate binding, allosteric Escherichia coli aspartate transcarbamoylase adopts alternate quaternary structures, stabilized by a set of interdomain and intersubunit interactions, which are readily differentiated by their solution x-ray scattering curves. The cooperative binding of aspartate in aspartate transcarbamoylase appears to result from the combination of the preexisting quaternary structure equilibrium with local changes induced by binding of carbamoyl phosphate | Escherichia coli | phosphate + N-carbamoyl-L-aspartate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
aspartate transcarbamoylase | - |
Escherichia coli |