EC Number |
Protein Variants |
Reference |
---|
3.2.1.169 | C166S |
site-directed mutagenesis |
702401 |
3.2.1.169 | C878S |
site-directed mutagenesis, comparable level of O-GlcNAcase activity as wild-type enzyme |
702401 |
3.2.1.169 | C896W |
site-specific mutagenesis, in the tryptic peptide LGCFEIAK (894-901). Site-specific mutagenesis of the C-terminal glycine and cysteine residues (G895A and C896W) present in the tryptic peptide LGCFEIAK (894901) causes little or no inhibition of O-GlcNAcase activity (72.3% of control and 129.9% of control, respectively) |
702152 |
3.2.1.169 | D174A |
generated mutant, reveals severely impaired catalytic activity across a broad range of substrates alongside a pH-activity profile consistent with deletion of a key catalytic residue |
702209 |
3.2.1.169 | D174N |
site-directed mutagenesis |
702401 |
3.2.1.169 | D175A |
generated mutant, significant decrease in catalytic efficiency with substrates bearing poor leaving groups (up to 3000fold), while for substrates bearing good leading groups the difference is much smaller (7fold). Mutant enzyme cleaves thioglycosides with essentially the same catalytic efficiency as the wild-type enzyme |
702209 |
3.2.1.169 | D175A |
site-directed mutagenesis |
702401 |
3.2.1.169 | D175N |
inactive |
751664 |
3.2.1.169 | D177N |
site-directed mutagenesis |
702401 |
3.2.1.169 | D242A |
site-directed mutant, 2800fold lower catalytic efficiency than wild-type |
705869 |