EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.5.1.15 | - |
Homo sapiens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.5.1.15 | N-acetyl-aspartate | decrease of the reaction rate at high substrate concentrations. Binding of N-acetyl-aspartate to the allosteric site induces significant rigidity to the protein loops with the amino acid side chains forming gates to the enzyme active site | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.15 | N-acetyl-L-aspartate + H2O | Homo sapiens | - |
acetate + L-aspartate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.15 | Homo sapiens | P45381 | - |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.15 | N-acetyl-L-aspartate + H2O | - |
Homo sapiens | acetate + L-aspartate | - |
? |