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Literature summary for 3.5.1.52 extracted from

  • Wang, S.; Xin, F.; Liu, X.; Wang, Y.; An, Z.; Qi, Q.; Wang, P.G.
    N-terminal deletion of peptide:N-glycanase results in enhanced deglycosylation activity (2009), PLoS ONE, 4, e8335.
    View publication on PubMedView publication on EuropePMC

Protein Variants

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

Organism UniProt Comment Textmining
Elizabethkingia meningoseptica
-
-
-
Saccharomyces cerevisiae
-
-
-
Schizosaccharomyces pombe
-
-
-

Substrates and Products (Substrate)

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

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
the optimum deglycosylation temperature of the Png1p-Rad23p complex is 30°C Saccharomyces cerevisiae

Temperature Stability [°C]

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

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

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