EC Number |
Protein Variants |
Reference |
---|
2.4.99.19 | D152E |
site-directed mutagenesis, D152 and E316 can both be mutated to their acidic counterparts (D152E and E316D) and still retain activity, albeit at a notably decreased level |
718913 |
2.4.99.19 | D154A |
the mutation reduces the observed glycosylation yield by over 50% compared to the wild-type enzyme |
720542 |
2.4.99.19 | D475A |
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme |
718913 |
2.4.99.19 | D475E |
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme |
718913 |
2.4.99.19 | D54A |
site-directed mutagenesis, the increased Und-PP-Bac-GalNAc substrate concentration has little effect on the mutant activity |
718913 |
2.4.99.19 | D56A |
the mutation reduces the observed glycosylation yield by over 90% compared to the wild-type enzyme |
720542 |
2.4.99.19 | D56A/E319A |
the double mutant is inactive |
720542 |
2.4.99.19 | E316D |
site-directed mutagenesis, D152 and E316 can both be mutated to their acidic counterparts (D152E and E316D) and still retain activity, albeit at a notably decreased level |
718913 |
2.4.99.19 | E316Q |
site-directed mutagenesis, inactive mutant |
718913 |
2.4.99.19 | E319A |
the mutation reduces the observed glycosylation yield by over 90% compared to the wild-type enzyme |
720542 |