EC Number   |
Protein Variants |
Reference |
|---|
    4.1.1.47 | E52Q |
site-directed mutagenesis |
705846 |
| 4.1.1.47 | I393A |
the mutation leads to a lower catalytic efficiency (3.9%) compared to the wild type enzyme. The enzyme is converted to an acetolactate synthase which can use pyruvate as a substrate with a catalytic efficiency (kcat/Km) of about 20times higher than that of the wild type enzyme |
727003 |
| 4.1.1.47 | I393V |
the mutation leads to a lower catalytic efficiency (5.3%) compared to the wild type enzyme |
727003 |
| 4.1.1.47 | I479V |
the mutation leads to a lower catalytic efficiency (4.8%) compared to the wild type enzyme |
727003 |
| 4.1.1.47 | L478A |
the mutation leads to a lower catalytic efficiency (0.34%) compared to the wild type enzyme |
727003 |
| 4.1.1.47 | V51D |
replacement of Val51 by an amino acid with a carboxylate in its side chain (glutamate or aspartate) has striking and significant effects, V51D variant of glyoxylate carboligase undergoes proton exchange at a rate 6fold higher than the wild-type enzyme |
703643 |
| 4.1.1.47 | V51D |
site-directed mutagenesis |
705846 |
| 4.1.1.47 | V51D |
the substitution shifts the pH optimum to 6.0-6.2, the mutant is less active (1.2%) than the wild type enzyme (turnover rates are 2 orders of magnitude lower) despite having higher rate of activation of the coenzyme |
727003 |
| 4.1.1.47 | V51D/I393A |
the enzyme is converted to an acetolactate synthase which can use pyruvate as a substrate with a catalytic efficiency (kcat/Km) of about 20times higher than that of the wild type enzyme |
727003 |
| 4.1.1.47 | V51E |
site-directed mutagenesis |
705846 |
