EC Number   |
Protein Variants |
Reference |
|---|
    2.5.1.18 | A113V |
wild type specific activity with 1-chloro-2,4-dinitrobenzene |
688419 |
| 2.5.1.18 | A122C |
the single-site mutation A122C and N124A/V (but not N124S/Y/C) restores the GST activity of Ure2p protein toward 1-chloro-2,4-dinitrobenzene, while causing a substantial reduction in glutathione peroxidase activity |
688426 |
| 2.5.1.18 | A140D |
naturally occuring mutation, most common missense polymorphism found in each of the populations studied so far, the substitution involves a charge change it does not seem to have a significant effect on enzymatic activity with a range of substrates |
721739 |
| 2.5.1.18 | A236V |
naturally occuring mutation, the substitution occurs in individuals from Chile and Mexico |
721739 |
| 2.5.1.18 | A85S |
a naturally occuring polymorphism in Caucasian population |
721739 |
| 2.5.1.18 | C101A |
site-directed mutagenesis, the mutant shows unaltered ligand binding compared to the wild-type enzyme |
677017 |
| 2.5.1.18 | C10A |
shows a 5 or 6fold higher kcat than wild type for both glutathione and 1-chloro-2,4-dinitrobenzene, accompanied by an 8fold increase in the Km for glutathione |
685020 |
| 2.5.1.18 | C10A |
the mutation causes the preferential binding of glutathione to the H-site, the mutant shows a decrease in activity of about 50%, drastic increase in Km value for glutathione of 105fold, and 23fold lower catalytic efficiency compared to the wild type enzyme |
689948 |
| 2.5.1.18 | C10A/S11A |
mutant shows dramatic decrease in specific activity of about 98%, the double mutation exhibits loss of affinity for glutathione, a Km value 10-fold higher than in the wild type, and a 291fold decrease of the catalytic efficiency compared to the wild type enzyme |
689948 |
| 2.5.1.18 | C10S |
shows a 25fold lower kcat for glutathione H and 5fold lower kcat for 1-chloro-2,4-dinitrobenzene than wild type accompanied by a 6fold decrease in the Km for glutathione |
685020 |
