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Information on EC 3.5.1.52 - peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase and Organism(s) Homo sapiens and UniProt Accession Q96IV0
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3.5.1.52 peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidaseIUBMB 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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Word Map
- 3.5.1.52
-
deglycosylation
- n-glycans
- lectin
- glycopeptides
-
sialic
-
endoglycosidase
- mannose
- neuraminidase
-
o-linked
- tunicamycin
-
sialylated
- n-acetylglucosamine
-
asparagine-linked
- fucose
- glcnac
-
concanavalin
-
high-mannose
- agglutinin
-
complex-type
-
fucosylated
- sialidase
-
glycoforms
-
endo-beta-n-acetylglucosaminidase
-
biantennary
-
glycomics
-
asn-linked
-
high-mannose-type
-
glycoproteomic
- n-acetyllactosamine
- almond
-
tetraantennary
- 2-aminopyridine
- meningosepticum
- n-glycoproteins
- endo-beta-galactosidase
- fetuin
- analysis
- keratanase
-
permethylated
-
3hglucosamine
-
hybrid-type
-
mannose-type
-
oligomannosidic
- synthesis
-
hydrazinolysis
- man9glcnac2
-
trifluoromethanesulfonic
-
pyridylaminated
-
high-ph
-
oligomannose
-
retrotranslocation
- neu5ac
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid PNGase M
-
-
-
-
glycopeptidase
-
-
-
-
glycopeptide N-glycosidase
-
-
-
-
jackbean glycopeptidase
-
-
-
-
L-929 PNGase
-
-
-
-
N-glycanase
-
-
-
-
N-oligosaccharide glycopeptidase
-
-
-
-
neutral PNGase M
-
-
-
-
peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F
-
-
-
-
PNGase A
-
-
-
-
PNGase At
-
-
-
-
PNGase F
-
-
-
-
PNGase J
-
-
-
-
PNGase Os
-
-
-
-
PNGase Se
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
83534-39-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glycoprotein US11 + H2O
?
-
the enzyme deglycolyzes HCMV glycoprotein US11
-
-
?
class I MHC HC + H2O
?
-
the enzyme is involved proteasomal degradation of glycosylated type I membrane protein class I MHC heavy chain, dislocated from ER to cytosol by cytomegalovirus-encoded glycoprotein US2 protein, overview
-
-
?
class I MHC HC + H2O
?
-
the enzyme deglycosylates dislocated membrane protein class I MHC heavy chain
-
-
?
tyrosinase + H2O
?
-
the enzyme is required for processing of a class I-restricted epitope from tyrosinase together with the cooperative action of endoplasmic reticulum aminopeptidase 1 and cytosolic protease, overview
-
-
?
tyrosinase + H2O
?
-
deglycosylation of tyrosinase at Asn371 and the Tyr369 epitope, reduced activity with tyrosinase peptides that are mutated in the glycosylation consensus sequence to give T373V mutants
-
-
?
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 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 deglycosylates misfolded glycoproteins, the enzyme is a mediator for p97 functions, the PUB domain functions as a p97 binding module in human enzyme, p97 is an AAA ATPase with an ubiquitin-selective molecular machine involved in multiple cellular processes including protein degradation through the ubiquitin-proteasome system
-
-
?
additional information
?
-
-
the enzyme is responsible for deglycosylation of N-linked glycoproteins dislocated from endoplasmic reticulum to cytosol
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
class I MHC HC + H2O
?
-
the enzyme is involved proteasomal degradation of glycosylated type I membrane protein class I MHC heavy chain, dislocated from ER to cytosol by cytomegalovirus-encoded glycoprotein US2 protein, overview
-
-
?
tyrosinase + H2O
?
-
the enzyme is required for processing of a class I-restricted epitope from tyrosinase together with the cooperative action of endoplasmic reticulum aminopeptidase 1 and cytosolic protease, overview
-
-
?
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 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 deglycosylates misfolded glycoproteins, the enzyme is a mediator for p97 functions, the PUB domain functions as a p97 binding module in human enzyme, p97 is an AAA ATPase with an ubiquitin-selective molecular machine involved in multiple cellular processes including protein degradation through the ubiquitin-proteasome system
-
-
?
additional information
?
-
-
the enzyme is responsible for deglycosylation of N-linked glycoproteins dislocated from endoplasmic reticulum to cytosol
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
carbobenzyloxy-Val-Ala-Asp-alpha-fluoromethylketone
-
i.e. Z-VAD-fmk, in vivo inhibition
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are severe developmental delay. An exome analysis identified a human patient with mutations in the NGLY1 gene and an increasing number of the patients harbouring mutations in NGLY1 alleles have been reported since then. The patients exhibited multiple symptoms that include global developmental delay, multifocal epilepsy, involuntary movement, abnormal liver function and the absence of tears
physiological function
Fbs1, a glycoprotein-specific ubiquitin ligase, protects misfolded glycoproteins from the action of cytoplasmic PNGase
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NGLY1_HUMAN
654
0
74390
Swiss-Prot
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the PUB domain, comprising residues 11-109, functions as a p97 binding module in human enzyme, three-dimensional structure of the PUB domain
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified wild-type PUB domain, also as selenomethionine variants, by sitting drop vapour diffusion method at 17°C, with a reservoir solution containing 0.2 M sodium acetate, 0.1 M Tris, pH 8.5, 30% PEG 4000, using 20% glycerol as cryoprotectant, X-ray diffraction structure determination and analysis at 1.6 A resolution, mutant L66M/L75M/L87M PUB domain are crystallized in 50% PEG 400, 0.1 M CHES, pH 9.5, 0.2 M NaCl, molecular replacement, X-ray diffraction structure determination and analysis at 1.9 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L66M/L75M/L87M
-
site-directed mutagenesis, the PUB domain mutant shows slightly reduced p97 binding
additional information
-
construction of PNGase U-373MG siRNA cell lines, the glycosylated type I membrane protein class I MHC HC, dislocated by US2 protein, becomes cytosolic when peptide: N-glycanase is compromised, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzyme fusion PUB domain from Escherichia coli strain C41(DE3) by nickel affinity chromatography, ion exchange chromatography, and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzyme PUB domain, comprising residues 11-109, fused to the lipoyl domain of Bacillus stearothermophilus dehihydrolipoamide acetyltransferase in Escherichia coli strain C41(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Blom, D.; Hirsch, C.; Stern, P.; Tortorella, D.; Ploegh, H.L.
A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised
EMBO J.
23
650-658
2004
Homo sapiens
Allen, M.D.; Buchberger, A.; Bycroft, M.
The PUB domain functions as a p97 binding module in human peptide N-glycanase
J. Biol. Chem.
281
25502-25508
2006
Homo sapiens
Altrich-VanLith, M.L.; Ostankovitch, M.; Polefrone, J.M.; Mosse, C.A.; Shabanowitz, J.; Hunt, D.F.; Engelhard, V.H.
Processing of a class I-restricted epitope from tyrosinase requires peptide N-glycanase and the cooperative action of endoplasmic reticulum aminopeptidase 1 and cytosolic protease
J. Immunol.
177
5440-5450
2006
Homo sapiens
Unal, E.S.; Zhao, R.; Qiu, A.; Goldman, I.D.
N-linked glycosylation and its impact on the electrophoretic mobility and function of the human proton-coupled folate transporter (HsPCFT)
Biochim. Biophys. Acta
1778
1407-1414
2008
Homo sapiens
Chantret, I.; Fasseu, M.; Zaoui, K.; Le Bizec, C.; Yaye, H.S.; Dupre, T.; Moore, S.E.
Identification of roles for peptide: N-glycanase and endo-beta-N-acetylglucosaminidase (Engase1p) during protein N-glycosylation in human HepG2 cells
PLoS ONE
5
e11734
2010
Homo sapiens
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)
EXTERNAL LINKS (specific for EC-Number 3.5.1.52)
Transporter Classification Database (TCDB): 3.A.16.1.5
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