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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.19D152E 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
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.19D154A the mutation reduces the observed glycosylation yield by over 50% compared to the wild-type enzyme 720542
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.19D475A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme 718913
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.19D475E site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme 718913
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.19D54A site-directed mutagenesis, the increased Und-PP-Bac-GalNAc substrate concentration has little effect on the mutant activity 718913
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.19D56A the mutation reduces the observed glycosylation yield by over 90% compared to the wild-type enzyme 720542
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.19D56A/E319A the double mutant is inactive 720542
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.19E316D 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
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.19E316Q site-directed mutagenesis, inactive mutant 718913
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.19E319A the mutation reduces the observed glycosylation yield by over 90% compared to the wild-type enzyme 720542
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