EC Number   |
Protein Variants |
Reference |
|---|
   5.1.3.7 | A209H |
mutant enzyme shows very limited epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine and slightly reduced epimerization activity with UDP-D-glucose and UDP-D-galactose |
661001 |
| 5.1.3.7 | A209H |
site-directed mutagenesis, the mutation results in limited ability to epimerize acetylated residues |
747460 |
| 5.1.3.7 | A209H |
unlike the wild-type enzyme the mutant enzyme is more efficient in catalyzing the reaction with the non-acetylated hexoses UDP-glucose and UDP-galactose than in catalyzing epimerization of UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine |
662221 |
| 5.1.3.7 | A209N |
mutant enzyme shows slightly reduced epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine and very limited epimerization activity with UDP-D-glucose and UDP-D-galactose |
661001 |
| 5.1.3.7 | A209N |
site-directed mutagenesis, the mutation enhances the specificity for acetylated substrates accompanied by a lower catalytic efficiency |
747460 |
| 5.1.3.7 | C300Y |
site-directed mutagenesis, the mutation results in decreased activity toward UDP-GlcNAc and UDP-GalNAc |
-, 747049 |
| 5.1.3.7 | G102K |
mutant enzyme shows slightly reduced epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine and no epimerization activity with UDP-D-glucose and UDP-D-galactose |
661001 |
| 5.1.3.7 | G102K |
site-directed mutagenesis, the mutation slightly reduces activity on acetylated substrates and almost abolishes activity on non-acetylated substrates |
747460 |
| 5.1.3.7 | G102K/Q201E |
site-directed mutagenesis, as a result of the introduction of both mutations at the same time, a salt bridge is formed, which results in a rescue of the activity for acetylated substrates, probably due to restoration of the slight distortion that is observed in both single mutants |
747460 |
| 5.1.3.7 | G118A/G119A |
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates |
726782 |
