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Literature summary for 2.1.3.2 extracted from
- Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes (2017), Protein Sci., 26, 2221-2228 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| R105A | catalytic trimer mutant | 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 | - |
phosphate + N-carbamoyl-L-aspartate | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0A786 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| carbamoyl phosphate + L-aspartate | - |
Escherichia coli | phosphate + N-carbamoyl-L-aspartate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| aspartate transcarbamoylase | - |
Escherichia coli |
| ATCase | - |
Escherichia coli |
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Release 2023.1 (January 2023)
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