Protein Variants | Comment | Organism |
---|---|---|
additional information | deletion of the N-terminal H1 helix (Png1p-DH1) enhances the deglycosylation activity of peptide:N-glycanase towards denatured glycoproteins | Saccharomyces cerevisiae |
additional information | deletion of the N-terminal H1 helix (Png1p-DH1) enhances the deglycosylation activity of peptide:N-glycanase towards denatured glycoproteins | Schizosaccharomyces pombe |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Elizabethkingia meningoseptica | - |
- |
- |
Saccharomyces cerevisiae | - |
- |
- |
Schizosaccharomyces pombe | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | peptide:N-glycanase catalyzes the detachment of N-linked glycan chains from glycopeptides or glycoproteins by hydrolyzing the beta-aspartylglucosaminyl bond. PNGase can not deglycosylate correctly folded native glycoproteins, but catalyzes the deglycosylation of misfolded glycoproteins | Elizabethkingia meningoseptica | ? | - |
? | |
additional information | peptide:N-glycanase catalyzes the detachment of N-linked glycan chains from glycopeptides or glycoproteins by hydrolyzing the beta-aspartylglucosaminyl bond. PNGase can not deglycosylate correctly folded native glycoproteins, but catalyzes the deglycosylation of misfolded glycoproteins. The complex formed between peptide:N-glycanase and Rad23p exhibits enhanced deglycosylation activity | Saccharomyces cerevisiae | ? | - |
? | |
additional information | peptide:N-glycanase catalyzes the detachment of N-linked glycan chains from glycopeptides or glycoproteins by hydrolyzing the beta-aspartylglucosaminyl bond. PNGase can not deglycosylate correctly folded native glycoproteins, but catalyzes the deglycosylation of misfolded glycoproteins. The complex formed between peptide:N-glycanase and Rad23p exhibits enhanced deglycosylation activity | Schizosaccharomyces pombe | ? | - |
? | |
RNase B + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
RNase B + H2O | - |
Schizosaccharomyces pombe | ? | - |
? | |
RNase B + H2O | - |
Elizabethkingia meningoseptica | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
peptide:N-glycanase | - |
Saccharomyces cerevisiae |
peptide:N-glycanase | - |
Schizosaccharomyces pombe |
peptide:N-glycanase | - |
Elizabethkingia meningoseptica |
Png1p | - |
Saccharomyces cerevisiae |
Png1p | - |
Schizosaccharomyces pombe |
PNGase | - |
Saccharomyces cerevisiae |
PNGase | - |
Schizosaccharomyces pombe |
PNGase F | - |
Elizabethkingia meningoseptica |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
the optimum deglycosylation temperature of the Png1p-Rad23p complex is 30°C | Saccharomyces cerevisiae |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | 45 | Png1p is inactive at 37°C. In contrast, the Png1p-Rad23p complex still possesses enzymatic activity at 45°C | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
the optimum deglycosylation pH of the Png1p-Rad23p complex is pH 7.0 | Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
physiological function | the complex formed between peptide:N-glycanase and Rad23p exhibits enhanced deglycosylation activity, which suggests an important role for this enzyme in the misfolded glycoprotein degradation pathway in vivo | Saccharomyces cerevisiae |
physiological function | the complex formed between peptide:N-glycanase and Rad23p exhibits enhanced deglycosylation activity, which suggests an important role for this enzyme in the misfolded glycoprotein degradation pathway in vivo | Schizosaccharomyces pombe |
physiological function | the complex formed between peptide:N-glycanase and Rad23p exhibits enhanced deglycosylation activity, which suggests an important role for this enzyme in the misfolded glycoprotein degradation pathway in vivo | Elizabethkingia meningoseptica |