EC Number   |
Protein Variants |
Reference |
|---|
   3.2.1.49 | D217N |
a naturally occuring Schindler disease and/or Kanzaki disease mutation |
709530 |
| 3.2.1.49 | E193X |
a naturally occuring Schindler disease and/or Kanzaki disease mutation |
709530 |
| 3.2.1.49 | E325K |
a naturally occuring Schindler disease and/or Kanzaki disease mutation |
709530 |
| 3.2.1.49 | E325K |
less favourable binding energy compared to native enzyme. The mutant enzyme possesses reduced volume in the catalytic cleft as compared to native enzyme resulting in the change in substrate pose. Changes in root mean square fluctuation of residues involved in catalytic activity affects the active site in terms of conformational space, thereby resulting in the change in catalytic volume that eventually lead to altered substrate pose. The proximity of substrate (electrophilic C1 of hexose ring) towards the enzyme (O2 of ASP139) is inconsistent for the mutant as compared to native enzyme resulting in less favourable binding energy of substrate. The mutants has detrimental effects contributing to the pathogenesis of the disease |
750879 |
| 3.2.1.49 | E367K |
a naturally occuring Schindler disease and/or Kanzaki disease mutation |
709530 |
| 3.2.1.49 | more |
construction of mutants of each of the five N-linked glycosylation sites |
709530 |
| 3.2.1.49 | N124Q |
35% activity in comparison to 100% activity of wild-type enzyme |
655678 |
| 3.2.1.49 | N177Q |
48% activity in comparison to 100% activity of wild-type enzyme |
655678 |
| 3.2.1.49 | N201Q |
28% activity in comparison to 100% activity of wild-type enzyme |
655678 |
| 3.2.1.49 | N201Q |
site-directed mutagenesis, one of the proteins with the third N-linked carbohydrate attachment site is removed |
709530 |
