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Literature summary for 3.5.1.52 extracted from
- The N-terminus of yeast peptide: N-glycanase interacts with the DNA repair protein Rad23 (2004), Biochem. Biophys. Res. Commun., 323, 149-155.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| co-expression of His6-tagged full-length enzyme or truncated versions with full-length Rad23 Escherichia coli strain BL21(DE3) | Saccharomyces cerevisiae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme hydrolyzes the beta-aspartylglycosylamine bond of asparagine-linked glycopeptides and glycoproteins, releasing an intact oligosaccharide and generating an aspartic acid residue at the cleavage site, the N-terminus of the enzyme interacts with the DNA repair protein Rad23 detected by gel filtration and surface plasmon resonance, quantitation of complex formation | Saccharomyces cerevisiae | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PNGase | - |
Saccharomyces cerevisiae |
| yeast peptide: N-glycanase | - |
Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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