EC Number   |
Natural Substrates |
|---|
   3.2.1.169 | more |
catalyzes the cleavage of beta-O-linked N-acetyl-beta-D-glucosaminide from modified proteins and is a member of the family 84 glycoside hydrolases |
| 3.2.1.169 | more |
catalyzing the hydrolytic cleavage of beta-O-linked 2-acetamido-2-deoxy-D-glycopyranose (O-GlcNAc) from serine and threonine residues of posttranslationally modified proteins |
| 3.2.1.169 | more |
enzyme cleaves 4-nitrophenyl N-acetyl-beta-D-glucosaminide from modified proteins and also cleaves 4-nitrophenyl N-acetyl-beta-D-thioglucosaminide |
| 3.2.1.169 | more |
enzyme is responsible for removal of the O-GlcNAc post-translational modification, is being increasingly used to aid in discerning the roles played by this form of intracellular glycosylation |
| 3.2.1.169 | more |
enzyme removes N-acetyl-beta-D-glucosaminide from proteins |
| 3.2.1.169 | more |
enzyme that removes N-acetyl-beta-D-glucosamine from O-GlcNAcylated proteins |
| 3.2.1.169 | more |
enzyme that removes O-GlcNAc from O-GlcNAcylated proteins |
| 3.2.1.169 | more |
has O-GlcNAcase activity against O-GlcNAcylated human proteins, suggesting that the enzyme is a suitable model for further studies into the function of human O-GlcNAcase |
| 3.2.1.169 | more |
O-GlcNAcase uses a catalytic mechanism involving substrate-assisted catalysis. In this mechanism, the leaving group is expelled from the anomeric center by nucleophilic attack of the 2-acetamido group of the substrate to form an oxazoline intermediate |
| 3.2.1.169 | more |
removes O-N-acetyl-glucosamine residues from O-GlcNAcylated proteins |
