EC Number   |
Protein Variants |
Reference |
|---|
   3.5.1.103 | D146A |
below 0.4% of wild-type activity |
720006 |
| 3.5.1.103 | D146A |
inactive mutant enzyme |
-, 752756 |
| 3.5.1.103 | D146A |
the D146N mutant is about 10fold higher than that of the D146A mutant, suggesting that the ability to accept a hydrogen bond at this position contributes to GlcNAc substrate specificity. Because there does not appear to be a direct contact between Asp146 and substrate, this effect is likely mediated via positioning of other catalytically important residues |
-, 752756 |
| 3.5.1.103 | D146N |
the D146N mutant is about 10fold higher than that of the D146A mutant, suggesting that the ability to accept a hydrogen bond at this position contributes to GlcNAc substrate specificity. Because there does not appear to be a direct contact between Asp146 and substrate, this effect is likely mediated via positioning of other catalytically important residues. The mutant enzyme shows 3.7% of the activity compared to the wild-type enzyme with the substrate N-acetyl-D-glucosamine |
-, 752756 |
| 3.5.1.103 | D15A |
0.5% of wild-type activity |
720006 |
| 3.5.1.103 | D15A |
the mutant enzyme shows 0.5% of the activity compared to the wild-type enzyme with the substrate N-acetyl-D-glucosamine |
752756 |
| 3.5.1.103 | D95A |
inactive mutant enzyme |
752756 |
| 3.5.1.103 | E47A |
the mutant enzyme shows 300% of the activity compared to the wild-type enzyme with the substrate N-acetyl-D-glucosamine. Mutation decreases the value of KM GlcNAc (2-fold) and increases the value of kcat/KM GlcNAc (3-fold) |
-, 752756 |
| 3.5.1.103 | F216A |
the mutant enzyme shows 110% of the activity compared to the wild-type enzyme with the substrate N-acetyl-D-glucosamine |
752756 |
| 3.5.1.103 | H144A |
1.0% of wild-type activity |
720006 |
