Crystallization (Comment) | Organism |
---|---|
two nearly identical crystal structures of the complexes between (S)-4-amino-4,5-dihydro-2-furancarboxylic acid and L-AspAT obtained at pH 7.5 and 8 are shown. The inhibitor forms only one adduct with the enzyme, with active site lysine 246, thus irreversibly inactivating the L-AspAT transamination reaction | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(S)-4-amino-4,5-dihydro-2-furancarboxylic acid | crystal structures of the Escherichi coli aspartate aminotransferase with (S)-4-amino-4,5-dihydro-2-furancarboxylic acid bound to the active site are obtained via cocrystallization at pH 7.5 and 8. The complex structures suggest that (S)-4-amino-4,5-dihydro-2-furancarboxylic acid inhibits the transamination reaction by forming adducts with the catalytic lysine 246 via a covalent bond while producing 1 equivalent of pyridoxamine 5'-phosphate | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | D3H0F7 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate + 2-oxoglutarate | - |
Escherichia coli | oxaloacetate + L-glutamate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
L-AspAT | - |
Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Escherichia coli |