EC Number   |
Protein Variants |
Reference |
|---|
    2.4.2.22 | E198D |
increases the turnover rates of the xanthine phosphoribosyltransferase without altering purine nucleobase specificity, converts the xanthine phosphoribosyltransferase into a broad-specificity enzyme capable of utilizing guanine, hypoxanthine, and xanthine as substrates. Can accommodate GMP in the active site |
704046 |
| 2.4.2.22 | E198D/E215D |
catalyzes robust guanine phosphoribosylation. Exhibits similar kinetic parameters in the presence of Mg2+ or Mn2+ as the wild-type. Substitution of Mg2+ with Mn2+ does not alter the hypoxanthine phosphoribosylation activity |
704046 |
| 2.4.2.22 | E215D |
increases the turnover rates of the xanthine phosphoribosyltransferase without altering purine nucleobase specificity, converts the xanthine phosphoribosyltransferase into a broad-specificity enzyme capable of utilizing guanine, hypoxanthine, and xanthine as substrates. Can accommodate GMP in the active site |
704046 |
| 2.4.2.22 | E215Q |
can accommodate GMP in the active site |
704046 |
| 2.4.2.22 | more |
deletion of the glycosomal targeting sequence, a C-terminal tripeptide, leads to mislocation of the enzyme in the cytosol, where the enzyme nevertheless is still active |
659904 |
| 2.4.2.22 | W181F |
the mutant retains its ability to catalyse the phosphoribosylation of hypoxanthine, guanine and xanthine, albeit with significantly lower specific activities than the wild type enzyme. The mutant shows an increase in Km for 5-phospho-alpha-D-ribose 1-diphosphate by 3.4fold under unactivated condition and a decrease in catalytic efficiency by 76fold under activated condition as compared to that of the wild type enzyme |
760104 |
| 2.4.2.22 | W181S |
the mutant retains its ability to catalyse the phosphoribosylation of hypoxanthine, guanine and xanthine, albeit with significantly lower specific activities than the wild type enzyme. The mutant shows 10fold reduced xanthine phosphoribosylation activity compared to the wild type enzyme |
760104 |
| 2.4.2.22 | W181S |
the mutant retains its ability to catalyze the phosphoribosylation of hypoxanthine, guanine and xanthine, albeit with significantly lower specific activities than the wild type enzyme. The mutant shows an increase in Km for 5-phospho-alpha-D-ribose 1-diphosphate by 2.1fold under unactivated condition and a decrease in catalytic efficiency by more than 11fold under activated condition as compared to that of the wild type enzyme |
760104 |
| 2.4.2.22 | W181Y |
the mutant retains its ability to catalyse the phosphoribosylation of hypoxanthine, guanine and xanthine, albeit with significantly lower specific activities than the wild type enzyme. The mutant shows an increase in Km for 5-phospho-alpha-D-ribose 1-diphosphate by 2.6fold under unactivated condition and a decrease in catalytic efficiency by more than 5fold under activated condition as compared to that of the wild type enzyme |
760104 |
