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Literature summary extracted from
- Location and characterization of the O-GlcNAcase active site (2006), Biochim. Biophys. Acta, 1760, 829-839.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.169 | construction of a pUC118-pTM hybrid expression vector containing the full length and splice variant mouse NCOAT | Mus musculus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.2.1.169 | C166S | site-directed mutagenesis | Mus musculus |
| 3.2.1.169 | C878S | site-directed mutagenesis, comparable level of O-GlcNAcase activity as wild-type enzyme | Mus musculus |
| 3.2.1.169 | D174N | site-directed mutagenesis | Mus musculus |
| 3.2.1.169 | D175A | site-directed mutagenesis | Mus musculus |
| 3.2.1.169 | D177N | site-directed mutagenesis | Mus musculus |
| 3.2.1.169 | DELTA250-345 | protein missing amino acids 250-345, due to the removal of exon 8 | Mus musculus |
| 3.2.1.169 | DELTA250-398 | lacks amino acids 250-398 in the protein due to the specific excision of exons 8 and 9 | Mus musculus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.169 | HPDP-biotin | treatment with a sulfhydrylspecific biotinylation reagent, HPDP-biotin, to biotinylate any accessible free cysteine residue in the native enzyme. Treatment is able to inhibit enzymatic activity, suggesting that the cysteine residue playing a role in catalysis is modified | Mus musculus |  |
| 3.2.1.169 | N-ethylmaleimide | treatment is able to inhibit enzymatic activity, suggesting that the cysteine residue playing a role in catalysis is modified | Mus musculus | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.169 | 0.26 | - |
4-nitrophenyl N-acetyl-beta-D-glucosaminide | D177N mutant | Mus musculus | |
| 3.2.1.169 | 0.46 | - |
4-nitrophenyl N-acetyl-beta-D-glucosaminide | C166S mutant | Mus musculus | |
| 3.2.1.169 | 0.49 | - |
4-nitrophenyl N-acetyl-beta-D-glucosaminide | wild-type | Mus musculus | |
| 3.2.1.169 | 0.97 | - |
4-nitrophenyl N-acetyl-beta-D-glucosaminide | D174N mutant | Mus musculus | |
| 3.2.1.169 | 1.4 | - |
4-nitrophenyl N-acetyl-beta-D-glucosaminide | D175A mutant | Mus musculus | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.169 | Mus musculus | Q9EQQ9 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.169 | - |
Mus musculus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.169 | 4-methylumbelliferyl N-acetyl-beta-D-glucosaminide + H2O | - |
Mus musculus | 4-methylumbelliferone + N-acetyl-beta-D-glucosamine | - |
? | |
| 3.2.1.169 | 4-nitrophenyl N-acetyl-beta-D-glucosaminide + H2O | - |
Mus musculus | 4-nitrophenol + N-acetyl-beta-D-glucosamine | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.169 | mNCOAT | - |
Mus musculus |
| 3.2.1.169 | NCOAT | bifunctional nucleo-cytoplasmic protein with both O-GlcNAcase and histone acetyltransferase domains | Mus musculus |
| 3.2.1.169 | O-GlcNAcase | - |
Mus musculus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.169 | 37 | - |
assay at | Mus musculus |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.169 | 2.3 | - |
4-nitrophenyl N-acetyl-beta-D-glucosaminide | D177N mutant | Mus musculus | |
| 3.2.1.169 | 6.4 | - |
4-nitrophenyl N-acetyl-beta-D-glucosaminide | D175A mutant | Mus musculus | |
| 3.2.1.169 | 18.6 | - |
4-nitrophenyl N-acetyl-beta-D-glucosaminide | D174N mutant | Mus musculus | |
| 3.2.1.169 | 21.7 | - |
4-nitrophenyl N-acetyl-beta-D-glucosaminide | C166S mutant | Mus musculus | |
| 3.2.1.169 | 54.9 | - |
4-nitrophenyl N-acetyl-beta-D-glucosaminide | wild-type | Mus musculus | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.169 | 5 | 5.5 | D174N mutant displayed a reduced catalytic efficiency at the wild type enzyme's optimal pH as well as in the basic pH range. It exhibits a marked shift in pH optimum to the pH 5-5.5 range | Mus musculus |
| 3.2.1.169 | 6.5 | 7 | optimum for the wild-type enzyme | Mus musculus |
| 3.2.1.169 | 7 | - |
assay at | Mus musculus |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.169 | 4.6 | - |
4-nitrophenyl N-acetyl-beta-D-glucosaminide | D175A mutant | Mus musculus | |
| 3.2.1.169 | 8.8 | - |
4-nitrophenyl N-acetyl-beta-D-glucosaminide | D177N mutant | Mus musculus | |
| 3.2.1.169 | 19.2 | - |
4-nitrophenyl N-acetyl-beta-D-glucosaminide | D174N mutant | Mus musculus | |
| 3.2.1.169 | 47.2 | - |
4-nitrophenyl N-acetyl-beta-D-glucosaminide | C166S mutant | Mus musculus | |
| 3.2.1.169 | 112 | - |
4-nitrophenyl N-acetyl-beta-D-glucosaminide | wild-type | Mus musculus | |
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