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Literature summary for 3.5.1.52 extracted from

  • Zhao, G.; Li, G.; Zhou, X.; Matsuo, I.; Ito, Y.; Suzuki, T.; Lennarz, W.J.; Schindelin, H.
    Structural and mutational studies on the importance of oligosaccharide binding for the activity of yeast PNGase (2009), Glycobiology, 19, 118-125.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.52

Cloned(Commentary)

Cloned (Comment) Organism
into the vector pET28a for expression in Escherichia coli BL21DE3 Codon Plus RIL cells Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystal structure of PNGase in complex with N,N'-diacetylchitobiose is described, refined at 3.4 A Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
D217A mutation in the peptide binding site Saccharomyces cerevisiae
E238A mutation in the chitobiose binding site Saccharomyces cerevisiae
H218A mutation in the chitobiose binding site Saccharomyces cerevisiae
H218F mutation in the chitobiose binding site Saccharomyces cerevisiae
K253A mutation in the chitobiose binding site Saccharomyces cerevisiae
N178A mutation in the peptide binding site Saccharomyces cerevisiae
Q239A mutation near the nonreducing end of the chitobiose, possible mannose binding site Saccharomyces cerevisiae
Q243A mutation near the nonreducing end of the chitobiose, possible mannose binding site Saccharomyces cerevisiae
R176A mutation in the peptide binding site Saccharomyces cerevisiae
W123A mutation in the peptide binding site Saccharomyces cerevisiae
W251A mutation in the chitobiose binding site Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
N-benzyloxycarbonyl-VAD-fluoromethylketone Z-VAD-fmk Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum endoplasmic reticulum-associated Saccharomyces cerevisiae 5783
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae catalyses the de-glycosylation of unfolded glycoproteins ?
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q02890
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Leu-Asn(GlcNAc5Man3Gal3)-Asp-Ser-Arg + H2O fetuin-derived asialoglycopeptide I, 14C, substrate activity assay Saccharomyces cerevisiae ?
-
 ?
additional information catalyses the de-glycosylation of unfolded glycoproteins Saccharomyces cerevisiae ?
-
 ?

Synonyms

Synonyms Comment Organism
peptide:N-glycanase
-
 Saccharomyces cerevisiae
PNGase
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 activity assay Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 activity assay Saccharomyces cerevisiae