EC Number   |
Protein Variants |
Reference |
|---|
    1.1.99.31 | G81A |
higher specificity for small substrates, compared to that of wild-type enzyme, the affinity for (S)-mandelate is relatively unchanged. The rate of the first half-reaction is slower than the wild-type rate. 2fold increase in oxidative half-reaction. Affinity for oxygen increases 10-15fold |
667577 |
| 1.1.99.31 | G81A |
mutation in the catalytically similar chimera MDH-GOX2 (mandelate dehydrogenase/glycolate oxidase), mutant has lower reactivity with substrate |
695329 |
| 1.1.99.31 | G81A |
wild type, mutant has lower reactivity with substrate |
695329 |
| 1.1.99.31 | G81D |
extreme low activity, reduction in activity is due to the decrease in electrophilicity of the FMN |
667577 |
| 1.1.99.31 | G81S |
the rate of the first half-reaction is slower than the wild-type rate. The rate of the first half-reaction is slower than the wild-type rate. Affinity for O2 increases 10-15fold |
667577 |
| 1.1.99.31 | G81V |
extreme low activity, reduction in activity is due to the decrease in electrophilicity of the FMN |
667577 |
| 1.1.99.31 | H274A |
inactive mutant, activity can partially be restored by the addition of exogenous imidazole |
667566 |
| 1.1.99.31 | H274D |
inactive mutant |
667566 |
| 1.1.99.31 | H274G |
inactive mutant, activity can be restored by the addition of exogenous imidazole |
667566 |
| 1.1.99.31 | more |
chimeric mutant of (S)-mandelate dehydrogenase with membrane anchoring loop replaced by a portion of glycolate oxidase from spinach is soluble and retains partial catalytic activity (about 1%) using (S)-mandelate as substrate. The activities of the soluble mutant enzymes (S)-mandelate dehydrogenase with residues 2-4 deleted and (S)-mandelate dehydrogenase with 17 residues deleted at the carboxy terminus are nearly the same when (S)-phenyllactate is used as substrate |
667564 |
