EC Number |
Protein Variants |
Reference |
---|
1.4.3.16 | E121A |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, catalytically inactive against either 3-OH-erythro- or 3-OH-threo-L-aspartate, but is active with N-acetyl- and N-formyl-L-aspartate |
711324 |
1.4.3.16 | E121D |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, catalytically inactive against either 3-OH-erythro- or 3-OH-threo-L-aspartate |
711324 |
1.4.3.16 | E121K |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, catalytically inactive against either 3-OH-erythro- or 3-OH-threo-L-aspartate |
711324 |
1.4.3.16 | E121Q |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, catalytically inactive against either 3-OH-erythro- or 3-OH-threo-L-aspartate |
711324 |
1.4.3.16 | H244A |
binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate |
391762 |
1.4.3.16 | H244A |
the mutant shows reduced catalytic efficiency compared to the wild type enzyme |
725741 |
1.4.3.16 | H244S |
binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate |
391762 |
1.4.3.16 | H351A |
binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate |
391762 |
1.4.3.16 | H351A |
inactive |
725741 |
1.4.3.16 | H351S |
binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate |
391762 |