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Literature summary for 3.5.1.52 extracted from

  • Li, G.; Zhao, G.; Zhou, X.; Schindelin, H.; Lennarz, W.J.
    The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor (2006), Proc. Natl. Acad. Sci. USA, 103, 8348-8353.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
co-expression of His-tagged or GST-tagged truncated enzyme variants and of GST-tagged enzyme mutants with His-tagged p97, transient co-expression and complex formatin of N-terminal GFP-tagged PNGase and c-myc-tagged AMFR in COS-1 cells Mus musculus

Protein Variants

Protein Variants Comment Organism
G79/F80A site-directed mutagenesis, the double mutation completely abolishes the interaction of PNGase with p97 Mus musculus
additional information construction of truncated enzyme variants comprising amino acid residues 1-80, 35-81, 1-181, 1-181DELTAPUB, 1-130, 1-111, 112-450, and 451-651 Mus musculus
N41P site-directed mutagenesis, the mutation completely abolishes the interaction of PNGase with p97 Mus musculus
N58A site-directed mutagenesis, the mutation does not affect the interaction of PNGase with p97 Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
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Mus musculus 5829
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus the enzyme removes N-linked oligosaccharides from misfolded glycoproteins as part of endoplasmic reticulum-associated degradation pathway involving a complex formation with proteins HR23B, cytosolic protein Y33K, p97, and autocrine motility factor receptor AMFR, the AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase AMFR, the N-terminus of PNGase interacts with the C-terminal tail of AMFR, complex formation model, overview ?
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?

Organism

Organism UniProt Comment Textmining
Mus musculus
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme removes N-linked oligosaccharides from misfolded glycoproteins as part of endoplasmic reticulum-associated degradation pathway involving a complex formation with proteins HR23B, cytosolic protein Y33K, p97, and autocrine motility factor receptor AMFR, the AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase AMFR, the N-terminus of PNGase interacts with the C-terminal tail of AMFR, complex formation model, overview Mus musculus ?
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?

Subunits

Subunits Comment Organism
More the N-terminus of PNGase interacts with the C-terminal tail of AMFR, and PNGase interacts with protein p97 essentially requiring the enzymes' PUB domain, overview, complex formation model, overview Mus musculus

Synonyms

Synonyms Comment Organism
peptide N-glycanase
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Mus musculus
PGNase
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Mus musculus