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HR23-ubiquitin-like domain + H2O
?
the N-terminal domain of PNGase (PUB) interacts with HR23-ubiquitin-like domain and ubiquitin chains
-
-
?
asialoglycopeptide I + H2O
?
-
fetuin-derived radio-labeled substrate, deglycosylation
-
-
?
bovine fetuin glycopeptide + H2O
?
denatured ribonuclease B + H2O
?
-
-
-
-
?
fetuin glycopeptide + H2O
?
-
-
-
-
?
additional information
?
-
ATPase p97 + H2O
?
a cofactor-binding motif of p97 contained within the last 10 amino acid residues of the C terminus is both necessary and sufficient to mediate interactions of p97 with PNGase. Phosphorylation of p97s highly conserved penultimate tyrosine residue, which is the main phosphorylation site during T cell receptor stimulation, completely blocks binding of either PNGase or Ufd3 to p97. This observation suggests that phosphorylation of this residue modulates endoplasmic reticulum-associated protein degradation activity by discharging substrate-processing cofactors
-
-
?
ATPase p97 + H2O
?
a cofactor-binding motif of p97 contained within the last 10 amino acid residues of the C terminus is both necessary and sufficient to mediate interactions of p97 with PNGase
-
-
?
bovine fetuin glycopeptide + H2O
?
-
-
-
-
?
bovine fetuin glycopeptide + H2O
?
-
Leu-Asn(Man3Gal3GlcNAc5)-Asp-Ser-Arg
-
-
?
additional information
?
-
the cytoplasmic PNGase in mammals is able to bind to p97/VCP/Cdc48, a key ATPases accosiated with diverse cellular activities (AAA) adenosine triphosphate (ATPase) for the ERAD pathway, as well as other ERAD or ubiquitinx02proteasome pathway-related proteins, some of which are intrinsic membrane proteins
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
the enzyme is responsible for deglycosylation of N-linked glycoproteins dislocated from endoplasmic reticulum to cytosol
-
-
?
additional information
?
-
-
the enzyme mediates the binding of the cytoplasmic proteins p97 and HR23B to the proteasome through formation of a ternary complex, p97 binds the autocrine motility factor receptor AMFR, modeling of interaction of the endoplasmic reticulum with the proteasome, overview
-
-
?
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
-
-
?
additional information
?
-
-
the enzyme removes N-linked oligosaccharides from misfolded glycoproteins as part of endoplasmic reticulum-associated degradation pathway involving a tight complex-formation with protein HR23, HR23 is also involved in DNA repair, co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways, overview
-
-
?
additional information
?
-
-
the enzyme deglycosylates misfolded proteins in the cytosol and shows multiple modes of interaction with the proteasome, overview
-
-
?
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ATPase p97 + H2O
?
a cofactor-binding motif of p97 contained within the last 10 amino acid residues of the C terminus is both necessary and sufficient to mediate interactions of p97 with PNGase. Phosphorylation of p97s highly conserved penultimate tyrosine residue, which is the main phosphorylation site during T cell receptor stimulation, completely blocks binding of either PNGase or Ufd3 to p97. This observation suggests that phosphorylation of this residue modulates endoplasmic reticulum-associated protein degradation activity by discharging substrate-processing cofactors
-
-
?
additional information
?
-
additional information
?
-
the cytoplasmic PNGase in mammals is able to bind to p97/VCP/Cdc48, a key ATPases accosiated with diverse cellular activities (AAA) adenosine triphosphate (ATPase) for the ERAD pathway, as well as other ERAD or ubiquitinx02proteasome pathway-related proteins, some of which are intrinsic membrane proteins
-
-
?
additional information
?
-
-
the enzyme is responsible for deglycosylation of N-linked glycoproteins dislocated from endoplasmic reticulum to cytosol
-
-
?
additional information
?
-
-
the enzyme mediates the binding of the cytoplasmic proteins p97 and HR23B to the proteasome through formation of a ternary complex, p97 binds the autocrine motility factor receptor AMFR, modeling of interaction of the endoplasmic reticulum with the proteasome, overview
-
-
?
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
-
-
?
additional information
?
-
-
the enzyme removes N-linked oligosaccharides from misfolded glycoproteins as part of endoplasmic reticulum-associated degradation pathway involving a tight complex-formation with protein HR23, HR23 is also involved in DNA repair, co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways, overview
-
-
?
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carbobenzyloxy-Val-Ala-Asp
-
i.e. Z-VAD, binds to the active site of the enzyme, binding structure, overview
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
Fbs1
-
Fbs1 captures malfolded glycoproteins, protecting them from the attack of PNGase, during the chaperoning or ubiquitinating operation in the cytosol
-
fucose residue alpha-1-3-linked or alpha-1-6-linked to the proximal GlnNAc residue
-
complete inhibition
-
liberated glycan reaction product
-
N,N'-diacetylchitobiose
-
GlcNAc2, competitive inhibitor may be directly accessible to the catalytic site
N-ethylmaleimide
-
2 mM, significant inhibition by thiol-modification, alkylation
Glycoasparagine
-
-
Glycoasparagine
-
1 mM causes 86% inhibition
liberated glycan reaction product
-
-
-
liberated glycan reaction product
-
causes 82% inhibition
-
Monoiodoacetic acid
-
2 mM causes 64% inhibition
Monoiodoacetic acid
-
2 mM, significant inhibition by thiol-modification
triomannose
-
-
triomannose
-
evidence for occupation of the carbohydrate-binding site
additional information
-
no effect: free peptides formed during reaction, mannose, alpha-methyl-D-mannoside, 5 mM Na2SO4
-
additional information
-
no effect: free peptides formed during reaction, mannose, alpha-methyl-D-mannoside, 5 mM Na2SO4
-
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C306A
-
site-directed mutagenesis, inactive mutant, inhibitor Z-VAD-fmk does not bind to the mutant enzyme
G79/F80A
-
site-directed mutagenesis, the double mutation completely abolishes the interaction of PNGase with p97
N41P
-
site-directed mutagenesis, the mutation completely abolishes the interaction of PNGase with p97
N58A
-
site-directed mutagenesis, the mutation does not affect the interaction of PNGase with p97
additional information
-
construction of truncated enzyme variants comprising amino acid residues 1-171, 1-471, 471-651, 171-471, 1-111, 112-450, 451-651, and 1-450
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
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Suzuki, T.; Seko, A.; Kitajima, K.; Inoue, Y.; Inoue, S.
Purification and enzymatic properties of peptide:N-glycanase from C3H mouse-derived L-929 fibroblast cells
J. Biol. Chem.
269
17611-17618
1994
Elizabethkingia meningoseptica, Oryzias latipes, Mus musculus
brenda
Suzuki, T.; Kitajima, K.; Inoue, S.; Inoue, Y.
Does an animal peptide N:glycanase have the dual role as an enzyme and a carbohydrate binding protein?
Glycoconj. J.
11
469-476
1994
Elizabethkingia meningoseptica, Oryzias latipes, Mus musculus, Prunus amygdalus var. dulcis
brenda
Kitajima, K.; Suzuki, T.; Kouchi, Z.; Inoue, S.; Inoue, Y.
Identification and distribution of peptide:N-glycanase (PNGase) in mouse organs
Arch. Biochem. Biophys.
319
393-401
1995
Mus musculus
brenda
Suzuki, T.; Kitajima, K.; Inoue, Y.; Inoue, S.
Carbohydrate-binding property of peptide:N-glycanase from mouse fibroblast L-929 cells as evaluated by inhibition and binding experiments using various oligosaccharides
J. Biol. Chem.
270
15181-15186
1995
Elizabethkingia meningoseptica, Mus musculus, Prunus amygdalus var. dulcis
brenda
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
Chem. Biol.
11
1677-1687
2004
Saccharomyces cerevisiae, Homo sapiens, Mus musculus
brenda
Zhao, G.; Zhou, X.; Wang, L.; Li, G.; Kisker, C.; Lennarz, W.J.; Schindelin, H.
Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways
J. Biol. Chem.
281
13751-13761
2006
Mus musculus
brenda
Li, G.; Zhou, X.; Zhao, G.; Schindelin, H.; Lennarz, W.J.
Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasome
Proc. Natl. Acad. Sci. USA
102
15809-15814
2005
Mus musculus
brenda
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
Proc. Natl. Acad. Sci. USA
103
8348-8353
2006
Mus musculus
brenda
Yamaguchi, Y.; Hirao, T.; Sakata, E.; Kamiya, Y.; Kurimoto, E.; Yoshida, Y.; Suzuki, T.; Tanaka, K.; Kato, K.
Fbs1 protects the malfolded glycoproteins from the attack of peptide:N-glycanase
Biochem. Biophys. Res. Commun.
362
712-716
2007
Mus musculus
brenda
Zhao, G.; Zhou, X.; Wang, L.; Li, G.; Schindelin, H.; Lennarz, W.J.
Studies on peptide:N-glycanase-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradation
Proc. Natl. Acad. Sci. USA
104
8785-8790
2007
Mus musculus (Q9JI78)
brenda
Suzuki, T.
Cytoplasmic peptide:N-glycanase and catabolic pathway for free N-glycans in the cytosol
Semin. Cell Dev. Biol.
18
762-769
2007
Arabidopsis thaliana, Saccharomyces cerevisiae, Mus musculus
brenda
Kamiya, Y.; Uekusa, Y.; Sumiyoshi, A.; Sasakawa, H.; Hirao, T.; Suzuki, T.; Kato, K.
NMR characterization of the interaction between the PUB domain of peptide:N-glycanase and ubiquitin-like domain of HR23
FEBS Lett.
586
1141-1146
2012
Mus musculus (Q9JI78)
brenda
Suzuki, T.
The cytoplasmic peptide N-glycanase (Ngly1) - basic science encounters a human genetic disorder
J. Biochem.
157
23-34
2015
Oryzias latipes, Neurospora crassa (D1MY48), Schizosaccharomyces pombe (O74739), Saccharomyces cerevisiae (Q02890), Saccharomyces cerevisiae, Dictyostelium discoideum (Q55FC8), Drosophila melanogaster (Q7KRR5), Homo sapiens (Q96IV0), Homo sapiens, Arabidopsis thaliana (Q9FGY9), Mus musculus (Q9JI78), Caenorhabditis elegans (Q9TW67), Schizosaccharomyces pombe ATCC 24843 (O74739), Schizosaccharomyces pombe 972 (O74739), Saccharomyces cerevisiae ATCC 204508 (Q02890)
brenda