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Literature summary for 3.5.1.52 extracted from
- NMR characterization of the interaction between the PUB domain of peptide:N-glycanase and ubiquitin-like domain of HR23 (2012), FEBS Lett., 586, 1141-1146.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21(DE3) Codon-Plus cells | Mus musculus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | Q9JI78 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| glutathione-Sepharose column chromatography | Mus musculus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| HR23-ubiquitin-like domain + H2O | the N-terminal domain of PNGase (PUB) interacts with HR23-ubiquitin-like domain and ubiquitin chains | Mus musculus | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| peptide:N-glycanase | - |
Mus musculus |
| PNGase | - |
Mus musculus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the N-terminal domain of PNGase (PUB) serves as a possible activator of HR23 in endoplasmic reticulum-associated degradation mechanisms | Mus musculus |
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