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Literature summary for 3.5.1.52 extracted from

  • Misaghi, S.; Pacold, M.; Blom, D.; Ploegh, H.L.; Korbel, G.A.
    Using a small molecule inhibitor of peptide:N-glycanaseto probe its role in glycoprotein turnover (2004), Chem. Biol., 11, 1677-1687.
    View publication on PubMed
Search for more literature for 3.5.1.52

Cloned(Commentary)

Cloned (Comment) Organism
expression of HA-tagged wild-type and mutant enzymes in U373 astrocytoma cells Mus musculus
expression of the enzyme in U373 astrocytoma cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
C191A site-directed mutagenesis, inactive mutant, inhibitor Z-VAD-fmk does not bind to the mutant enzyme Saccharomyces cerevisiae
C306A site-directed mutagenesis, inactive mutant, inhibitor Z-VAD-fmk does not bind to the mutant enzyme Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
carbobenzyloxy-Val-Ala-Asp-alpha-fluoromethylketone i.e. Z-VAD-fmk, a broad-spectrum caspase inhibitor, binds covalently to the active site of the mammalian enzyme, in vivo inhibition of recombinant PNGase in U373 cells, overview Homo sapiens
carbobenzyloxy-Val-Ala-Asp-alpha-fluoromethylketone i.e. Z-VAD-fmk, a broad-spectrum caspase inhibitor, binds covalently to the active site of the mammalian enzyme Mus musculus
carbobenzyloxy-Val-Ala-Asp-alpha-fluoromethylketone i.e. Z-VAD-fmk, a broad-spectrum caspase inhibitor, IC50: 0.05 mM, binds covalently to the active site of the yeast enzyme, no restoration of enzyme activity by dialysis Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Mus musculus 5829
-
cytosol
-
 Homo sapiens 5829
-
cytosol
-
 Saccharomyces cerevisiae 5829
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43208
-
 x * 43208, MALDI mass spectrometry Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus the enzyme is responsible for deglycosylation of N-linked glycoproteins dislocated from endoplasmic reticulum to cytosol ?
-
 ?
additional information Homo sapiens the enzyme is responsible for deglycosylation of N-linked glycoproteins dislocated from endoplasmic reticulum to cytosol ?
-
 ?
additional information Saccharomyces cerevisiae the enzyme is responsible for deglycosylation of N-linked glycoproteins dislocated from endoplasmic reticulum to cytosol ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mus musculus
-
 gene png1
-
Saccharomyces cerevisiae
-
 gene png1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycoprotein US11 + H2O the enzyme deglycolyzes HCMV glycoprotein US11 Homo sapiens ?
-
 ?
glycoprotein US2 + H2O the enzyme deglycolyzes HCMV glycoprotein US2 Homo sapiens ?
-
 ?
additional information the enzyme is responsible for deglycosylation of N-linked glycoproteins dislocated from endoplasmic reticulum to cytosol Mus musculus ?
-
 ?
additional information the enzyme is responsible for deglycosylation of N-linked glycoproteins dislocated from endoplasmic reticulum to cytosol Homo sapiens ?
-
 ?
additional information the enzyme is responsible for deglycosylation of N-linked glycoproteins dislocated from endoplasmic reticulum to cytosol Saccharomyces cerevisiae ?
-
 ?
RNase B + H2O the enzyme deglycolyzes RNaseB Saccharomyces cerevisiae ?
-
 ?

Subunits

Subunits Comment Organism
? x * 43208, MALDI mass spectrometry Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
MPng1
-
 Mus musculus
peptide:N-glycanase
-
 Mus musculus
peptide:N-glycanase
-
 Homo sapiens
peptide:N-glycanase
-
 Saccharomyces cerevisiae
PNGase
-
 Mus musculus
PNGase
-
 Homo sapiens
PNGase
-
 Saccharomyces cerevisiae
PNGase F
-
 Mus musculus
PNGase F
-
 Saccharomyces cerevisiae
YPng1
-
 Saccharomyces cerevisiae

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.05
-
 i.e. Z-VAD-fmk, a broad-spectrum caspase inhibitor, IC50: 0.05 mM, binds covalently to the active site of the yeast enzyme, no restoration of enzyme activity by dialysis Saccharomyces cerevisiae carbobenzyloxy-Val-Ala-Asp-alpha-fluoromethylketone