EC Number |
Inhibitors |
Structure |
---|
2.6.1.1 | (2-chloro-6-[[(3,5-dimethyl-4H-1,2,4-triazol-4-yl)imino-kappaN]methyl]phenolato-kappaO)(2-[[(3-methyl-4H-1,2,4-triazol-4-yl)imino-kappaN]methyl]phenolato-kappaO)copper |
- |
|
2.6.1.1 | (2-[[(3,5-dimethyl-4H-1,2,4-triazol-4-yl)imino-kappaN]methyl]phenolato-kappaO)(2-hydroxyethyl)(2-[[(3-methyl-4H-1,2,4-triazol-4-yl)imino-kappaN]methyl]phenolato-kappaO)cuprate(1-) |
- |
|
2.6.1.1 | (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 |
|
2.6.1.1 | 1-(2,4-dichlorophenyl)-3-[2-(1H-indol-3-yl)ethyl]urea |
- |
|
2.6.1.1 | 1-(4-chlorophenyl)-3-[2-(1H-indol-3-yl)ethyl]urea |
- |
|
2.6.1.1 | 1-biphenyl-2-yl-3-[2-(1H-indol-3-yl)ethyl]urea |
- |
|
2.6.1.1 | 1-[2-(1H-indol-3-yl)ethyl]-3-phenylurea |
- |
|
2.6.1.1 | 1-[2-(1H-indol-3-yl)ethyl]-3-[3-(trifluoromethyl)phenyl]urea |
- |
|
2.6.1.1 | 1-[2-(1H-indol-3-yl)ethyl]-3-[4-(trifluoromethyl)phenyl]urea |
- |
|
2.6.1.1 | 2-methyl-DL-aspartate |
binds to the pyridoxal 5'-phosphate form of the enzyme, formation of an external aldimine complex |
|