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Information on EC 3.5.1.52 - peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase and Organism(s) Mus musculus and UniProt Accession Q9JI78

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EC Tree
IUBMB Comments
Does not act on (GlcNAc)Asn, because it requires the presence of more than two amino-acid residues in the substrate [cf. EC 3.5.1.26, N4-(beta-N-acetylglucosaminyl)-L-asparaginase]. The plant enzyme was previously erroneously listed as EC 3.2.2.18.
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This record set is specific for:
Mus musculus
UNIPROT: Q9JI78
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
n-glycanase, pngase f, n-glycosidase f, pngase, peptide n-glycosidase f, ngly1, peptide-n-glycosidase f, glycopeptidase, peptide:n-glycosidase, peptide:n-glycanase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
peptide:N-glycanase
-
acid PNGase M
-
-
-
-
glycopeptidase
-
-
-
-
glycopeptide N-glycosidase
-
-
-
-
jackbean glycopeptidase
-
-
-
-
L-929 PNGase
-
-
-
-
MPng1
-
-
N-glycanase
-
-
-
-
N-oligosaccharide glycopeptidase
-
-
-
-
neutral PNGase M
-
-
-
-
peptide N-glycanase
-
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peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F
-
-
-
-
peptide:N-glycanase
-
-
PNGase A
-
-
-
-
PNGase At
-
-
-
-
PNGase F
PNGase J
-
-
-
-
PNGase Os
-
-
-
-
PNGase Se
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of an N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue
show the reaction diagram
active site structure and catalytic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic acid amide
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
N-linked-glycopeptide-(N-acetyl-beta-D-glucosaminyl)-L-asparagine amidohydrolase
Does not act on (GlcNAc)Asn, because it requires the presence of more than two amino-acid residues in the substrate [cf. EC 3.5.1.26, N4-(beta-N-acetylglucosaminyl)-L-asparaginase]. The plant enzyme was previously erroneously listed as EC 3.2.2.18.
CAS REGISTRY NUMBER
COMMENTARY hide
83534-39-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATPase p97 + H2O
?
show the reaction diagram
HR23-ubiquitin-like domain + H2O
?
show the reaction diagram
the N-terminal domain of PNGase (PUB) interacts with HR23-ubiquitin-like domain and ubiquitin chains
-
-
?
asialoglycopeptide I + H2O
?
show the reaction diagram
-
fetuin-derived radio-labeled substrate, deglycosylation
-
-
?
bovine fetuin glycopeptide + H2O
?
show the reaction diagram
denatured ribonuclease B + H2O
?
show the reaction diagram
-
-
-
-
?
fetuin glycopeptide + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATPase p97 + H2O
?
show the reaction diagram
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 p97’s 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
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
dependent on
Zn2+
-
zinc binding domain structure involving a CXXC motif, zinc binding stabilizes the enzyme conformation by stabilizing the intermediate state and promoting product release
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Z-VAD-fmk
-
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
-
Glycoasparagine
liberated glycan reaction product
-
Monoiodoacetic acid
N,N'-diacetylchitobiose
-
GlcNAc2, competitive inhibitor may be directly accessible to the catalytic site
N-ethylmaleimide
-
2 mM, significant inhibition by thiol-modification, alkylation
triomannose
yeast mannan
-
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.114
Fetuin glycopeptide
-
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
-
liver PNGase
6.8
-
spleen PNGase
7
-
L-929 PNGase, brain PNGase, kidney PNGase
7.2
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
-
no activity below 5.5
6.8 - 7
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 37
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
C3H mouse-derived L-929 fibroblast cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
minor distribution of Ngly1 in the membrane fraction
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NGLY1_MOUSE
651
0
74275
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105000
-
2 * 105000, homodimer, SDS-PAGE, 41% content of hydrophobic acids
212000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion, crystal structure of the N-terminal domain of PNGase in complex with the cofactor-binding motif of p97 contained within the last 10 amino acid residues of the C terminus provides detailed insight into the interaction between p97 and its substrate-processing cofactors
purified recombinant enzyme core domain and XPCB domain in complex with the recombinant murine HR23B protein, 9.5 mg/ml of enzyme domains in a 1:1 ratio, vapour diffusion method, against reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 28-32% PEG 4000, 0.2 M sodium acetate, heavy atom derivatization by soaking in 1 mM ethyl mercury thiosalicylate, 1 mM K2[PtCN4], or 1 mM KAuCN2 for 4 h, cryoprotection by 20% glycerol, X-ray diffraction structure determination and analysis at 1.85 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
rapidly reduced stability above 37°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
zinc binding stabilizes the enzyme conformation by stabilizing the intermediate state and promoting product release
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose column chromatography
460fold
-
recombinant full-length enzyme, enzyme core domain, and enzyme XPCB domain from Escherichia coli strain BL21(DE3),the XPCB domain by chitin affinity chromatographyand gel filtration
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recombinant GST-tagged proteasome components HR23B, S4, and AMFR from Escherichia coli by glutathione affinity batch method, recombinant His6-tagged wild-type enzyme and truncated variants from Escherichia coli by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) Codon-Plus cells
gene NGLY1, sequence comparisons and phylogenetic analysis
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
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co-expression of the His6-tagged wild-type enzyme and truncated variants with GST-tagged murine proteasome components HR23B, S4, and autocrine motility factor receptor AMFR in Escherichia coli
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expression of HA-tagged wild-type and mutant enzymes in U373 astrocytoma cells
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overexpression of the full-length enzyme, enzyme core domain, and enzyme XPCB domain in Escherichia coli strain BL21(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team