EC Number   |
Protein Variants |
Reference |
|---|
   1.17.3.2 | C1318Y |
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme |
689359 |
| 1.17.3.2 | C535A/C992R |
site-directed mutagenesis, the mutant activity in the presence of sulfhydryl residue modifiers is very low |
744875 |
| 1.17.3.2 | C535A/C992R/C1316S |
site-directed mutagenesis, the triple mutant does not undergo conversion from XOR, EC 1.17.3.2, to XDH, EC 1.17.1.4, at all |
744875 |
| 1.17.3.2 | C535A/C992R/C1324S |
site-directed mutagenesis, the triple mutant does not undergo conversion from XOR, EC 1.17.3.2, to XDH, EC 1.17.1.4, at all |
744875 |
| 1.17.3.2 | D1109T |
naturally occuring nonsynonymous single nucleotide polymorphism |
689359 |
| 1.17.3.2 | E1261X |
mutation of Glu1261 leads to a complete loss of activity |
716010 |
| 1.17.3.2 | E232A |
site-directed mutagenesis, the mutant exhibits a 12fold decrease in kred compared to wild-type |
745314 |
| 1.17.3.2 | E232Q |
site-directed mutagenesis, kred, the limiting rate constant for reduction at high [xanthine], is significantly compromised in the mutant variant E232Q, the mutant exhibits a 12fold decrease in kred, a result that is inconsistent with Glu232 being neutral in the active site of the wild-type enzyme |
745314 |
| 1.17.3.2 | E308V |
site-directed mutagenesis, mutant molybdopterin domain structure, overview, the xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site, the E803V mutation almost completely abrogates the activity towards hypoxanthine as a substrate, but the decrease in activity towards purine substrate is not due to large conformational change in the mutant enzyme |
674374 |
| 1.17.3.2 | E802Q |
site-directed mutagenesis, altered kinetics of the mutant enzyme compared to the wild-type enzyme |
716010 |
