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Literature summary for 2.6.1.1 extracted from
- Cofactor-directed reversible denaturation pathways: the cofactor-stabilized Escherichia coli aspartate aminotransferase homodimer unfolds through a pathway that differs from that of the apoenzyme (2007), Biochemistry, 46, 5819-5829.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| in the presence of 0.01 mM pyridoxal 5'-phosphate | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-aspartate + 2-oxoglutarate | - |
Escherichia coli | oxaloacetate + L-glutamate | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | - |
Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AATase | - |
Escherichia coli |
| aspartate aminotransferase | - |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | binds at the intersubunit active sites and stabilizes the native enzyme form | Escherichia coli | |
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