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Information on EC 3.5.1.52 - peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase
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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 expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
acid PNGase M, acidic peptide:N-glycanase, acidic PNGase, aPNGase, At3g14920, At5g05480, AtPNG1, DDB0189828, glycoamidase, glycopeptidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid PNGase M
-
-
-
-
acidic peptide:N-glycanase
aPNGase
At3g14920
At5g05480
glycopeptidase
-
-
-
-
glycopeptide N-glycosidase
-
-
-
-
jackbean glycopeptidase
-
-
-
-
L-929 PNGase
-
-
-
-
N-glycanase
N-oligosaccharide glycopeptidase
-
-
-
-
neutral PNGase M
-
-
-
-
Ngly1
peptide N-glycanase
peptide N-glycosidase
peptide-N-(N-acetyl-beta-glucosaminyl) asparagine amidase F
-
-
peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F
-
-
-
-
peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase
peptide: N-glycanase
peptide:N-glycanase
PGNase
PNG-1
PNG1
Png1p
PNGase
PNGase A
-
-
-
-
PNGase A-like enzyme
PNGase At
-
-
-
-
PNGase F
PNGase H+
PNGase J
-
-
-
-
PNGase Os
-
-
-
-
PNGase Se
-
-
-
-
PNGase Yl
PNGase-A
N-glycanase
-
-
-
-
peptide:N-glycanase
-
-
PNG1
-
wild type PNG1 has substitutions in essential catalytic amino acids, and its deglycosylation activity is lost
PNGase F
-
-
-
-
PNGase F
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
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
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
Asn-Asn(oligosaccharide)-Glu-Ser-Ser + H2O = Asn-Asp-Glu-Ser-Ser + 1-amino-N-acetylglucosamine-oligosaccharide, step 1, catalysed by the enzyme, 1-amino-N-acetylglucosamine-oligosaccharide + H2O = N-acetylglucosamine-oligosaccharide + NH3, step 2
Prunus amygdalus var. dulcis
-
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
mechanism and catalytic center
-
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
active site structure and catalytic mechanism
-
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
the catalytic triad is formed by Cys191, His218, and Asp235
-
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
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of carboxylic acid amide
-
-
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
83534-39-8
-
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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
alpha1-antitrypsin Pi Z + H2O
deglycosylated alpha1-antitrypsin Pi Z
-
-
-
?
Antithrombin III + H2O
?
-
significant amount of only partly de-N-glycosylated protein is detected even after more than 18 h incubation time with PNGase F
-
-
?
asialoglycopeptide I + H2O
?
-
fetuin-derived radio-labeled substrate, deglycosylation
-
-
?
bence-jones wh lambda glycopeptide + H2O
?
-
acid PNGase M from blastoderm stage 11
-
-
?
coagulation factor IX + H2O
?
-
almost quantitative de-N-glycosylation with PNGase F is observed after a rather short time
-
-
?
concanavalin A-precursor + H2O
?
-
deglycosylation leads to conversion into an active lectin
-
-
?
Cys-Gly-Leu-Val-Pro-Val-Leu-Ala-Glu-Asn-Tyr-Asn(Man3Gal2GlcNAc4NeuAc2)-Lys + H2O
?
-
-
-
?
dabcyl-Gly-Glu-Asn-(GlcNAcbeta(1->2)Manalpha(1->3)[GlcNAcbeta(1->2)Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta)-Arg + H2O
GlcNAcbeta(1->2)Manalpha(1->3)[GlcNAcbeta(1->2)Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + dabcyl-Gly-Glu-Asn-Arg
denatured RNase B + H2O
?
-
SpPNGase cleaves N-glycan from denatured RNase B
-
-
?
fetuin glycopeptide II + H2O
?
-
acid PNGase M from blastoderm stage 11
-
-
?
fetuin-derived asialoglycopeptide I + H2O
?
-
([14C]-CH3)2Leu-Asn(GlcNAc5-Man3Gal3)-Asp-Ser-Arg
-
-
?
glycoprotein US11 + H2O
?
-
the enzyme deglycolyzes HCMV glycoprotein US11
-
-
?
horse radish peroxidase + H2O
?
only PNGase F-II can release alpha->1,3 core-fucosylated glycans from HRP
-
-
?
HR23-ubiquitin-like domain + H2O
?
the N-terminal domain of PNGase (PUB) interacts with HR23-ubiquitin-like domain and ubiquitin chains
-
-
?
Leu-Asn(GlcNAc5Man3Gal3)-Asp-Ser-Arg + H2O
?
fetuin-derived asialoglycopeptide I, 14C, substrate activity assay
-
-
?
mu opioid receptor + H2O
?
-
the enzyme removes all N-linked glycans
-
-
?
N-glycoprotein + H2O
?
-
PNGase is involved in the release of N-glycans from N-glycoproteins
-
-
?
Oryzias latipes glycophosphoprotein MU-1 + H2O
?
-
acid PNGase M from blastoderm stage 11, yolk-absorptive stage
-
-
?
Oryzias latipes glycophosphoprotein MU-2 + H2O
?
-
acid PNGase M from blastoderm stage 11, yolk-absorptive stage
-
-
?
ovalbumin + H2O
?
-
deglycosylation of the heat-denatured protein
-
-
?
ovotransferrin glycopeptide + H2O
?
Prunus amygdalus var. dulcis
-
Gly-Leu-Ile-His-Asn(oligosaccharide)-Arg
-
-
?
receptor for advanced glycation end-products isoform H-300 + H2O
?
-
-
-
-
?
receptor for advanced glycation end-products isoform N-16 + H2O
?
-
-
-
-
?
ricin A + H2O
?
-
deglycosylation of ricin A, the enzyme acts in complex with protein Rad23, interaction and complex formation analysis, overview
-
-
?
RNAse + H2O
?
removes high mannose-type N-glycan from denatured RNase B, but not from native RNase B
-
-
?
RTADELTA protein + H2O
deglycosylated RTADELTA protein + ?
-
RTADELTA is a non-toxic mutant of ricin A-chain
-
-
?
RTADELTA-transmembrane-Leu2 protein + H2O
deglycosylated RTADELTA-transmembrane-Leu2 protein + ?
-
-
-
-
?
sialylglycopeptide + H2O
?
asialo-, agalactosyl-, trimannosyl- and monomanosyl-sialylglycopeptides are hydrolyzed
-
-
?
taka-amylase A + H2O
?
Prunus amygdalus var. dulcis
-
1,4-alpha-D-glucan glucanohydrolase, EC 3.2.1.1
-
-
?
XylMan3FucGlcNAc2-Asn-peptide from horse raddish peroxidase + H2O
?
-
-
-
-
?
yeast carboxypeptidase + H2O
?
-
deglycosylation of heat-denatured protein
-
-
?
alpha-dansyl derivative fetuin pentaglycopeptide + H2O
?
Prunus amygdalus var. dulcis
-
-
-
-
?
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 p97Ć¢ĀĀs 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
-
-
?
beta-aspartylglycosylamine + H2O
aspartic acid + NH3 + N-acetylglucosamine
-
1-L-beta-aspartamido-2-acetamido-1,2-dideoxy-beta-D-glucose
-
?
beta-aspartylglycosylamine + H2O
aspartic acid + NH3 + N-acetylglucosamine
-
1-L-beta-aspartamido-2-acetamido-1,2-dideoxy-beta-D-glucose
-
?
beta-aspartylglycosylamine + H2O
aspartic acid + NH3 + N-acetylglucosamine
-
1-L-beta-aspartamido-2-acetamido-1,2-dideoxy-beta-D-glucose
-
?
bovine fetuin glycopeptide + H2O
?
-
Leu-Ala-Asn-(oligosaccharide)-AeCys-Ser
-
-
?
bovine fetuin glycopeptide + H2O
?
-
Leu-Asn(Man3Gal3GlcNAc5)-Asp-Ser-Arg
-
-
?
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
-
-
?
dabcyl-Gly-Glu-Asn-(GlcNAcbeta(1->2)Manalpha(1->3)[GlcNAcbeta(1->2)Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta)-Arg + H2O
GlcNAcbeta(1->2)Manalpha(1->3)[GlcNAcbeta(1->2)Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + dabcyl-Gly-Glu-Asn-Arg
-
-
-
-
?
dabcyl-Gly-Glu-Asn-(GlcNAcbeta(1->2)Manalpha(1->3)[GlcNAcbeta(1->2)Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta)-Arg + H2O
GlcNAcbeta(1->2)Manalpha(1->3)[GlcNAcbeta(1->2)Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + dabcyl-Gly-Glu-Asn-Arg
-
-
-
-
?
glycopeptide + H2O
?
Prunus amygdalus var. dulcis
-
with 3-11 amino acid residues
-
-
?
ovalbumin glycopeptide + H2O
aspartic acid + NH3 + N-acetylglucosamine
-
Glu-Glu-Lys-Tyr-Asn(oligosaccharide)-Leu-Thr-Ser-Val
-
-
?
ovalbumin glycopeptide + H2O
aspartic acid + NH3 + N-acetylglucosamine
Prunus amygdalus var. dulcis
-
Glu-Glu-Lys-Tyr-Asn(oligosaccharide)-Leu-Thr-Ser-Val
-
?
ovalbumin glycopeptide + H2O
aspartic acid + NH3 + N-acetylglucosamine
-
Glu-Glu-Lys-Tyr-Asn(oligosaccharide)-Leu-Thr-Ser-Val
-
-
?
ovalbumin glycopeptide + H2O
aspartic acid + NH3 + N-acetylglucosamine
-
Glu-Glu-Lys-Tyr-Asn(oligosaccharide)-Leu-Thr-Ser-Val
-
?
pineapple stem bromelain glycopeptide + H2O
?
-
Asn-Asn-(oligosaccharide)-Glu-Ser-Ser
-
-
?
pineapple stem bromelain glycopeptide + H2O
?
-
Asn-Asn-(oligosaccharide)-Glu-Ser-Ser
-
-
?
pineapple stem bromelain glycopeptide + H2O
?
Prunus amygdalus var. dulcis
-
Asn-Asn-(oligosaccharide)-Glu-Ser-Ser
-
-
?
pineapple stem bromelain glycopeptide + H2O
?
-
Asn-Asn-(oligosaccharide)-Glu-Ser-Ser
-
-
?
ribonuclease B + H2O
?
-
no activity with bovine pancreatic ribonuclease B with oligomannose-type N-glycans at Asn-34. Native RNase BS, generated by subtilisin digestion of native RNase B, which comprises amino acid residues 21-124 of RNase B, is sensitive to PNGase F digestion. The same holds for carboxymethylated RNase. The structural basis of the difference in sensitivity for PNGase F in the de-N-glycosylation of the native bovine pancreatic ribonucleases B and BS is determined
-
-
?
ribonuclease B + H2O
?
-
When ribonuclease B is denatured at 60-65ĆĀŗC or by 40-60 mM dithiothreitol, its deglycosylation by Png1p is most prominent
-
-
?
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 AtPNG1 gene encodes a bona fide peptide:N-glycanase that contributes to ERAD related protein quality control in plants
-
-
?
additional information
?
-
-
PNG1 can function not only as peptide:N-glycanase but also as transglutaminase
-
-
?
additional information
?
-
development of an assay system for acidic peptide:N-glycanase (aPNGase) activity in crude plant extract using fluorescence-labeled N-glycopeptides as a substrates, overview. The enzyme produces free N-glycans
-
-
?
additional information
?
-
development of an assay system for acidic peptide:N-glycanase (aPNGase) activity in crude plant extract using fluorescence-labeled N-glycopeptides as a substrates, overview. The enzyme produces free N-glycans
-
-
?
additional information
?
-
development of an assay system for acidic peptide:N-glycanase (aPNGase) activity in crude plant extract using fluorescence-labeled N-glycopeptides as a substrates, overview. The enzyme produces free N-glycans
-
-
?
additional information
?
-
development of an assay system for acidic peptide:N-glycanase (aPNGase) activity in crude plant extract using fluorescence-labeled N-glycopeptides as a substrates, overview. The enzyme produces free N-glycans
-
-
?
additional information
?
-
-
PNG-1, the cytoplasmic PNGase orthologue, exhibits dual enzyme functions, not only as peptide:N-glycanase but also as an oxidoreductase(thioredoxin)
-
-
?
additional information
?
-
the enzyme catalyzes a deglycosylation reaction and cleaves at beta-aspartyl glucosylamine bond and removes complete glycan moiety from the glycoprotein substrate. Its reaction is different from transglutaminase catalyzed transamidating or amide bond formation reaction. The Dictyostelium discoideum PNGase is a functional peptide:N-glycanase enzyme possessing deglycosylation activity, but does not possess any significant transamidation activity
-
-
?
additional information
?
-
-
the enzyme catalyzes a deglycosylation reaction and cleaves at beta-aspartyl glucosylamine bond and removes complete glycan moiety from the glycoprotein substrate. Its reaction is different from transglutaminase catalyzed transamidating or amide bond formation reaction. The Dictyostelium discoideum PNGase is a functional peptide:N-glycanase enzyme possessing deglycosylation activity, but does not possess any significant transamidation activity
-
-
?
additional information
?
-
Dictyostelium discoideum NC-4 / ATCC 24697
the enzyme catalyzes a deglycosylation reaction and cleaves at beta-aspartyl glucosylamine bond and removes complete glycan moiety from the glycoprotein substrate. Its reaction is different from transglutaminase catalyzed transamidating or amide bond formation reaction. The Dictyostelium discoideum PNGase is a functional peptide:N-glycanase enzyme possessing deglycosylation activity, but does not possess any significant transamidation activity
-
-
?
additional information
?
-
-
the Drosophila ortholog of PNGase (PngI) does not possess deglycosylation activity but retains carbohydrate-binding activity. The transglutaminase domain of Pngl participates in some type of catalytic activity even though the protein does not have the conventional deglycosylation activity
-
-
?
additional information
?
-
-
PNGase F is responsible for deglycosylation of misfolded proteins, the reverse reaction, glycosylation of peptides RKDVY and EILDVPST by PNGase F, is also possible in vitro, determination of glycosylation sites by MALDI-TOF mass spectrometry, overview, in addition non-enzymatic glycosylation of sugars, which are more than two units long, occurs
-
-
?
additional information
?
-
-
the enzyme is a glycoaminidase cleaving the link between asparagine and N-acetylglucosamines
-
-
?
additional information
?
-
-
peptide:N-glycanase catalyzes the detachment of N-linked glycan chains from glycopeptides or glycoproteins by hydrolyzing the beta-aspartylglucosaminyl bond. PNGase can not deglycosylate correctly folded native glycoproteins, but catalyzes the deglycosylation of misfolded glycoproteins
-
-
?
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
-
-
?
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 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
-
-
?
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
?
-
development of an assay system for acidic peptide:N-glycanase (aPNGase) activity in crude plant extract using fluorescence-labeled N-glycopeptides as a substrates, overview
-
-
?
additional information
?
-
-
ability of enzyme to distinguish between native and misfolded substrates
-
?
additional information
?
-
-
overview on in vivo glycoprotein substrates
-
?
additional information
?
-
-
involved in proteasomal degradation of misfolded glycoproteins
-
?
additional information
?
-
-
the cytosolic enzyme deglycosylates misfolded glycoproteins prior to the endoplasmic reticulum-associated protein degradation
-
-
?
additional information
?
-
-
the enzyme is responsible for deglycosylation of N-linked glycoproteins dislocated from endoplasmic reticulum to cytosol
-
-
?
additional information
?
-
-
the deglycosylating enzyme catalyzes the hydrolysis of the beta-aspartylglycosylamine bond of asparagine-linked glycopeptides and glycoproteins, the misfolding or denaturation of glycoproteins is a prerequisite for enzyme activity
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the beta-aspartylglycosylamine bond of asparagine-linked glycopeptides and glycoproteins, releasing an intact oligosaccharide and generating an aspartic acid residue at the cleavage site, the N-terminus of the enzyme interacts with the DNA repair protein Rad23 detected by gel filtration and surface plasmon resonance, quantitation of complex formation
-
-
?
additional information
?
-
catalyses the de-glycosylation of unfolded glycoproteins
-
-
?
additional information
?
-
-
catalyses the de-glycosylation of unfolded glycoproteins
-
-
?
additional information
?
-
-
peptide:N-glycanase catalyzes the detachment of N-linked glycan chains from glycopeptides or glycoproteins by hydrolyzing the beta-aspartylglucosaminyl bond. PNGase can not deglycosylate correctly folded native glycoproteins, but catalyzes the deglycosylation of misfolded glycoproteins. The complex formed between peptide:N-glycanase and Rad23p exhibits enhanced deglycosylation activity
-
-
?
additional information
?
-
protein-protein interaction involving the cytoplasmic peptide:N-glycanase with DNA repair-related protein Rad23
-
-
?
additional information
?
-
-
protein-protein interaction involving the cytoplasmic peptide:N-glycanase with DNA repair-related protein Rad23
-
-
?
additional information
?
-
protein-protein interaction involving the cytoplasmic peptide:N-glycanase with DNA repair-related protein Rad23
-
-
?
additional information
?
-
-
SpPNGase deglycosylates the misfolded glycoproteins
-
-
?
additional information
?
-
-
peptide:N-glycanase catalyzes the detachment of N-linked glycan chains from glycopeptides or glycoproteins by hydrolyzing the beta-aspartylglucosaminyl bond. PNGase can not deglycosylate correctly folded native glycoproteins, but catalyzes the deglycosylation of misfolded glycoproteins. The complex formed between peptide:N-glycanase and Rad23p exhibits enhanced deglycosylation activity
-
-
?
additional information
?
-
the enzyme hydrolyses the beta-aspartyl-glycosylamine bond of N-linked glycoproteins/glycopeptides and releases free N-glycans
-
-
?
additional information
?
-
-
the enzyme hydrolyses the beta-aspartyl-glycosylamine bond of N-linked glycoproteins/glycopeptides and releases free N-glycans
-
-
?
additional information
?
-
development of an assay system for acidic peptide:N-glycanase (aPNGase) activity in crude plant extract using fluorescence-labeled N-glycopeptides as a substrates, overview. The enzyme produces free N-glycans
-
-
?
additional information
?
-
development of an assay system for acidic peptide:N-glycanase (aPNGase) activity in crude plant extract using fluorescence-labeled N-glycopeptides as a substrates, overview. The enzyme produces free N-glycans
-
-
?
additional information
?
-
-
heat-denatured RNase B and lactoferrin are almost completely deglycosylated by PNGaseH+, profiles of N-glycan products released from the substrates, similar to PNGase F, overview. The acidic enzyme, termed PNGase H+, shows an extremely low pH optimum with a broad substrate specificity. The recombinant PNGase H+ can liberate high mannose-, hybrid- and complex-type N-glycans including core alpha1,3-fucosylated oligosaccharides from both glycoproteins and glycopeptides. PNGase H+ exhibits a better release efficiency over N-glycans without core alpha1,3-fucose compared with PNGase A
-
-
?
additional information
?
-
-
heat-denatured RNase B and lactoferrin are almost completely deglycosylated by PNGaseH+, profiles of N-glycan products released from the substrates, similar to PNGase F, overview. The acidic enzyme, termed PNGase H+, shows an extremely low pH optimum with a broad substrate specificity. The recombinant PNGase H+ can liberate high mannose-, hybrid- and complex-type N-glycans including core alpha1,3-fucosylated oligosaccharides from both glycoproteins and glycopeptides. PNGase H+ exhibits a better release efficiency over N-glycans without core alpha1,3-fucose compared with PNGase A
-
-
?
additional information
?
-
-
using glycopeptide substrates, PNGase Yl releases various types of N-glycans including high-mannose and complex-type glycans as well as glycans containing core-linked alpha(1,3)-fucose that are frequently found in plants and insects. In comparison with PNGase A, PNGase Yl is able to cleave with higher efficiency the glycans from some denatured glycoproteins. PNGase Yl shows the highest activity toward HRP glycopeptides attached with trimannosyl core glycans containing beta(1,2)-xylose and core-linked alpha, substrate specificity, overview(1,3)-fucose
-
-
?
additional information
?
-
-
using glycopeptide substrates, PNGase Yl releases various types of N-glycans including high-mannose and complex-type glycans as well as glycans containing core-linked alpha(1,3)-fucose that are frequently found in plants and insects. In comparison with PNGase A, PNGase Yl is able to cleave with higher efficiency the glycans from some denatured glycoproteins. PNGase Yl shows the highest activity toward HRP glycopeptides attached with trimannosyl core glycans containing beta(1,2)-xylose and core-linked alpha, substrate specificity, overview(1,3)-fucose
-
-
?
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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
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 p97Ć¢ĀĀs 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
-
-
?
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
-
-
?
concanavalin A-precursor + H2O
?
-
deglycosylation leads to conversion into an active lectin
-
-
?
N-glycoprotein + H2O
?
-
PNGase is involved in the release of N-glycans from N-glycoproteins
-
-
?
Oryzias latipes glycophosphoprotein MU-1 + H2O
?
-
acid PNGase M from blastoderm stage 11, yolk-absorptive stage
-
-
?
Oryzias latipes glycophosphoprotein MU-2 + H2O
?
-
acid PNGase M from blastoderm stage 11, yolk-absorptive stage
-
-
?
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 AtPNG1 gene encodes a bona fide peptide:N-glycanase that contributes to ERAD related protein quality control in plants
-
-
?
additional information
?
-
the enzyme catalyzes a deglycosylation reaction and cleaves at beta-aspartyl glucosylamine bond and removes complete glycan moiety from the glycoprotein substrate. Its reaction is different from transglutaminase catalyzed transamidating or amide bond formation reaction. The Dictyostelium discoideum PNGase is a functional peptide:N-glycanase enzyme possessing deglycosylation activity, but does not possess any significant transamidation activity
-
-
?
additional information
?
-
-
the enzyme catalyzes a deglycosylation reaction and cleaves at beta-aspartyl glucosylamine bond and removes complete glycan moiety from the glycoprotein substrate. Its reaction is different from transglutaminase catalyzed transamidating or amide bond formation reaction. The Dictyostelium discoideum PNGase is a functional peptide:N-glycanase enzyme possessing deglycosylation activity, but does not possess any significant transamidation activity
-
-
?
additional information
?
-
Dictyostelium discoideum NC-4 / ATCC 24697
the enzyme catalyzes a deglycosylation reaction and cleaves at beta-aspartyl glucosylamine bond and removes complete glycan moiety from the glycoprotein substrate. Its reaction is different from transglutaminase catalyzed transamidating or amide bond formation reaction. The Dictyostelium discoideum PNGase is a functional peptide:N-glycanase enzyme possessing deglycosylation activity, but does not possess any significant transamidation activity
-
-
?
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
-
-
?
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 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 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
?
-
-
involved in proteasomal degradation of misfolded glycoproteins
-
?
additional information
?
-
-
the cytosolic enzyme deglycosylates misfolded glycoproteins prior to the endoplasmic reticulum-associated protein degradation
-
-
?
additional information
?
-
-
the enzyme is responsible for deglycosylation of N-linked glycoproteins dislocated from endoplasmic reticulum to cytosol
-
-
?
additional information
?
-
catalyses the de-glycosylation of unfolded glycoproteins
-
-
?
additional information
?
-
-
catalyses the de-glycosylation of unfolded glycoproteins
-
-
?
additional information
?
-
protein-protein interaction involving the cytoplasmic peptide:N-glycanase with DNA repair-related protein Rad23
-
-
?
additional information
?
-
-
protein-protein interaction involving the cytoplasmic peptide:N-glycanase with DNA repair-related protein Rad23
-
-
?
additional information
?
-
protein-protein interaction involving the cytoplasmic peptide:N-glycanase with DNA repair-related protein Rad23
-
-
?
additional information
?
-
-
SpPNGase deglycosylates the misfolded glycoproteins
-
-
?
additional information
?
-
the enzyme hydrolyses the beta-aspartyl-glycosylamine bond of N-linked glycoproteins/glycopeptides and releases free N-glycans
-
-
?
additional information
?
-
-
the enzyme hydrolyses the beta-aspartyl-glycosylamine bond of N-linked glycoproteins/glycopeptides and releases free N-glycans
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
additional information
Zn2+
bound at the C-terminus of the recombinant enzyme, Zn2+ is derived from the pET28a expression vector
Zn2+
-
zinc binding domain structure involving a CXXC motif, zinc binding stabilizes the enzyme conformation by stabilizing the intermediate state and promoting product release
additional information
the enzyme does not require any metal ions for full enzymatic activity
additional information
-
the enzyme does not require any metal ions for full enzymatic activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone
-
covalently bind to the active site Cys191 of recombinant yeast peptide N-glycanase
CuSO4
-
nearly complete inhibition of the acid PNGase M by 5 mM, 10-20% remaining activity at neutral PNGase M by 5 mM
Fbs1
-
Fbs1 captures malfolded glycoproteins, protecting them from the attack of PNGase, during the chaperoning or ubiquitinating operation in the cytosol
-
FeCl3
-
nearly complete inhibition of the acid PNGase M by 5 mM, 10-20% remaining activity at neutral PNGase M by 5 mM
fucose residue alpha-1-3-linked or alpha-1-6-linked to the proximal GlnNAc residue
-
complete inhibition
-
L-hyosphorin derived nonapeptide
-
1 mM causes 92% inbition of acid PNGase M
-
Man9GlcNAc2-iodoacetoamide
-
strong inhibitor, irreversibly inhibits that catalytic Cys in a highly specific manner
p-chloromercuribenzoic acid
-
0.5 mM causes 89% inhibition of neutral PNGase M
SDS
-
complete inactivation by 0.05% SDS can be corrected by the addition of 1% Nonidet P-40
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, in vivo inhibition of recombinant PNGase in U373 cells, overview
carbobenzyloxy-Val-Ala-Asp-alpha-fluoromethylketone
-
i.e. Z-VAD-fmk, in vivo inhibition
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
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
N,N'-diacetylchitobiose
-
GlcNAc2, competitive inhibitor may be directly accessible to the catalytic site
N-ethylmaleimide
-
2 mM, significant inhibition by thiol-modification, alkylation
Z-VAD-fmk
-
i.e. carbobenzyloxy-Val-Ala-Asp-alpha-fluoromethylketone, a broad-spectrum caspase inhibitor, potent inhibition, binding structure determination and analysis with wild-type and mutant C191A enzyme, the inhibitor binds covalently to the catalytic residue Cys191, but not to the catalytic His218
additional information
-
no effect: yeast mannan, trimannose
-
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
-
additional information
-
no effect: 1 mM peptide free N-linked glycan, 1 mM de-N-glycosylated peptide, 5 mM phenylmethylsulfonyl fluoride at neutral PNGase M; no effect: 5 mM monoiodoacetic acid, 0.5 mM p-chloromercurobenzoic acid, 5 mM ZnCl2 at acid PNGase M
-
additional information
Prunus amygdalus var. dulcis
-
no effect: thiol inhibitors, iodoacetamide, N-ethylmaleimide, actinomycete protease inhibitors, leupeptins, chymostatin, pepstatin, Mg2+, Ca2+, Mn2+, EDTA, L-cysteine, phenylmethylsulfonyl fluoride, gamma-D-gluconolactone, yeast mannan, triomannose
-
additional information
Prunus amygdalus var. dulcis
-
no effect: thiol inhibitors, iodoacetamide, N-ethylmaleimide, actinomycete protease inhibitors, leupeptins, chymostatin, pepstatin, Mg2+, Ca2+, Mn2+, EDTA, L-cysteine, phenylmethylsulfonyl fluoride, gamma-D-gluconolactone, yeast mannan, triomannose
-
additional information
Prunus amygdalus var. dulcis
-
no effect: thiol inhibitors, iodoacetamide, N-ethylmaleimide, actinomycete protease inhibitors, leupeptins, chymostatin, pepstatin, Mg2+, Ca2+, Mn2+, EDTA, L-cysteine, phenylmethylsulfonyl fluoride, gamma-D-gluconolactone, yeast mannan, triomannose
-
additional information
-
the enzyme is preferably inhibited by aspartate-based inhibitors
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DTT
-
10 mM, absence causes inactivation of L-929 PNGase, suggesting S-H group essential for enzyme activity
DTT
-
mouse organ-derived PNGase requires at least 1 mM DTT for maximal activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4
bromelain glycopeptide
Prunus amygdalus var. dulcis
-
stem bromelain undecapeptide, glycopeptidase group C
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
carbobenzyloxy-Val-Ala-Asp-alpha-fluoromethylketone
Saccharomyces cerevisiae
-
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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
5.5
6.5
6.6
7.2
7.5
7
-
the optimum deglycosylation pH of the Png1p-Rad23p complex is pH 7.0
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 3.5
-
remarkable loss of activity above pH 3.5, narrow pH range, profile overview
3 - 8.6
-
80% of the maximum activity at pH 3.3, 65% of the maximum activity at pH 8.6
4 - 7.5
-
pH 4.0: about 50% of maximal activity, pH 7.5: about 40% of maximal activity, surface-displayed PNGase F
5 - 10
-
pH 5: about 50% of maximal activity, pH 10.0: about 70% of maximal activity
6 - 9
-
pH 6: about 70% of maximal activity, pH 9.0: about 60% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
30
-
the optimum deglycosylation temperature of the Png1p-Rad23p complex is 30ĆĀ°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 37
-
20ĆĀ°C: about 60% of maximal activity, 37ĆĀ°C: about 55% of maximal activity
20 - 40
-
20ĆĀ°C: about 80% of maximal activity, 40ĆĀ°C: about 75% of maximal activity
20 - 45
-
20ĆĀ°C: about 50% of maximal activity, 45ĆĀ°C: about 60% of maximal activity, surface-displayed PNGase F
20 - 60
enzyme activity declines rapidly above 40ĆĀ°C (80% activity at 50ĆĀ°C, 55% activity at 60ĆĀ°C, 30% activity at 70ĆĀ°C, no activity at 80ĆĀ°C)
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Prunus amygdalus var. dulcis
almond
-
-
brenda
-
171678, 288921, 288922, 288923, 288924, 288927, 668438, 670850, 685226, 686438, 688656, 688824, 711705, 713354, 718792
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the highest activities are found in the youngest parts of the plant: apical buds, flowers and leaf blades
brenda
-
the highest activities are found in the youngest parts of the plant: apical buds, flowers and leaf blades
brenda
-
the highest activities are found in the youngest parts of the plant: apical buds, flowers and leaf blades
brenda
additional information
-
recombinantly expressed in Escherichia coli
brenda
additional information
-
the AtPNG1 gene is uniformly and constitutively expressed at low levels throughout all developmental stages of the plant
brenda
additional information
expression levels and patterns of Ddpngase are developmentally regulated. Higher level of enzyme expression during the aggregate stage. The expression gets restricted to the prestalk region during later developmental stages
brenda
additional information
-
expression levels and patterns of Ddpngase are developmentally regulated. Higher level of enzyme expression during the aggregate stage. The expression gets restricted to the prestalk region during later developmental stages
brenda
additional information
Dictyostelium discoideum NC-4 / ATCC 24697
-
expression levels and patterns of Ddpngase are developmentally regulated. Higher level of enzyme expression during the aggregate stage. The expression gets restricted to the prestalk region during later developmental stages
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
the recombinant fluorescent-tagged enzyme is also present to a lower extent in the cytosol
brenda
Dictyostelium discoideum NC-4 / ATCC 24697
-
the recombinant fluorescent-tagged enzyme is also present to a lower extent in the cytosol
-
brenda
-
membrane, catalytic site in luminal orientation
brenda
endoplasmic reticulum-associated
brenda
minor distribution of Ngly1 in the membrane fraction
brenda
minor distribution of Ngly1 in the membrane fraction
brenda
the recombinant fluorescent-tagged enzyme colocalizes in the nucleus along with DAPI blue stained DNA
brenda
Dictyostelium discoideum NC-4 / ATCC 24697
-
the recombinant fluorescent-tagged enzyme colocalizes in the nucleus along with DAPI blue stained DNA
-
brenda
additional information
localized in close proximity to the proteasomal machinery
-
brenda
additional information
-
localized in close proximity to the proteasomal machinery
-
brenda
additional information
Dictyostelium discoideum NC-4 / ATCC 24697
-
localized in close proximity to the proteasomal machinery
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
phylogenetic analysis of acidic PNGases, yeast PNGases are diverse and distantly related from filamentous fungi PNGases in the phylogenetic tree
evolution
the enzyme from Dictyostelium discoideum is a member of transglutaminase (TG) -like superfamily and shows presence of a common transglutaminase core domain and sequence homology with the known PNGases, the tertiary structure matches with the mouse PNGase. DdPNGase possess the catalytic triad residues Cys210, His237 and Asp252, corresponding to the conserved core residues of other PNGases. DdPNGase also possess the corresponding Trp239 and Trp248, Arg229 and Glu241 conserved residues which possibly are essential for catalysis
evolution
PNGases are classified into two types based on their optimum pH: neutral or cytosolic PNGase (cPNGase) and acidic PNGase (aPNGase). cPNGase is found ubiquitously in eukaryotic cells, while aPNGase is found mainly in plants
evolution
PNGases are classified into two types based on their optimum pH: neutral or cytosolic PNGase (cPNGase) and acidic PNGase (aPNGase). cPNGase is found ubiquitously in eukaryotic cells, while aPNGase is found mainly in plants
evolution
PNGases are classified into two types based on their optimum pH: neutral or cytosolic PNGase (cPNGase) and acidic PNGase (aPNGase). cPNGase is found ubiquitously in eukaryotic cells, while aPNGase is found mainly in plants
evolution
-
PNGases are classified into two types based on their optimum pH: neutral or cytosolic PNGase (cPNGase) and acidic PNGase (aPNGase). cPNGase is found ubiquitously in eukaryotic cells, while aPNGase is found mainly in plants
-
evolution
Dictyostelium discoideum NC-4 / ATCC 24697
-
the enzyme from Dictyostelium discoideum is a member of transglutaminase (TG) -like superfamily and shows presence of a common transglutaminase core domain and sequence homology with the known PNGases, the tertiary structure matches with the mouse PNGase. DdPNGase possess the catalytic triad residues Cys210, His237 and Asp252, corresponding to the conserved core residues of other PNGases. DdPNGase also possess the corresponding Trp239 and Trp248, Arg229 and Glu241 conserved residues which possibly are essential for catalysis
-
evolution
-
PNGases are classified into two types based on their optimum pH: neutral or cytosolic PNGase (cPNGase) and acidic PNGase (aPNGase). cPNGase is found ubiquitously in eukaryotic cells, while aPNGase is found mainly in plants
-
evolution
-
phylogenetic analysis of acidic PNGases, yeast PNGases are diverse and distantly related from filamentous fungi PNGases in the phylogenetic tree
-
malfunction
mutations in png-1 result in an increase in axon branching during morphogenesis of the vulval egg-laying organ and egg-laying behavior changes, neuronal defects include an increase in the branched morphology of the VC4 and VC5 egg-laying neurons as well as inappropriate branches from axons that run adjacent to the vulva
malfunction
an enzyme knockout results in small sized aggregates, all of which do not form fruiting bodies. Knockout mutants show defect in aggregation, penotypes, overview
malfunction
in yeast cells, the absence of cytoplasmic PNGase (Png1) results in significant reduction of the levels of free oligosaccharidesfound in the cytosol, suggesting that the majority, if not all, of the free oligosaccharidesin yeast are generated from misfolded glycoproteins in a PNGase-dependent manner. Phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are defect in ERAD, but no growth/viability defects
malfunction
phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are abnormal axon branching of VC4/VC5 egg-laying neurons, and egg-laying behaviour defect
malfunction
phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are global developmental delay, movement disorder, and hypotonia
malfunction
phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are not detected
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
malfunction
phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are slow growth and development, as well as defect in cell aggregation during multicellular development
malfunction
phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are temperature-sensitive growth with strong polarity defects
malfunction
Dictyostelium discoideum NC-4 / ATCC 24697
-
an enzyme knockout results in small sized aggregates, all of which do not form fruiting bodies. Knockout mutants show defect in aggregation, penotypes, overview
-
malfunction
-
in yeast cells, the absence of cytoplasmic PNGase (Png1) results in significant reduction of the levels of free oligosaccharidesfound in the cytosol, suggesting that the majority, if not all, of the free oligosaccharidesin yeast are generated from misfolded glycoproteins in a PNGase-dependent manner. Phenotypes/pathological conditions caused by mutations in gene orthologues of cytoplasmic PNGase are defect in ERAD, but no growth/viability defects
-
metabolism
the enzyme is proposed to participate in the proteasome dependent glycoprotein degradation pathway
metabolism
acidic peptide:N-glycanase (aPNGase) plays a pivotal role in plant glycoprotein turnover
metabolism
acidic peptide:N-glycanase (aPNGase) plays a pivotal role in plant glycoprotein turnover
metabolism
acidic peptide:N-glycanase (aPNGase) plays a pivotal role in plant glycoprotein turnover
metabolism
-
acidic peptide:N-glycanase (aPNGase) plays a pivotal role in plant glycoprotein turnover
-
metabolism
Dictyostelium discoideum NC-4 / ATCC 24697
-
the enzyme is proposed to participate in the proteasome dependent glycoprotein degradation pathway
-
metabolism
-
acidic peptide:N-glycanase (aPNGase) plays a pivotal role in plant glycoprotein turnover
-
physiological function
png-1 can act from both neurons and epithelial cells to restrict axon branching. PNGase and Rad-23 regulate neuronal branching during organ innervation
physiological function
-
the complex formed between peptide:N-glycanase and Rad23p exhibits enhanced deglycosylation activity, which suggests an important role for this enzyme in the misfolded glycoprotein degradation pathway in vivo
physiological function
-
the complex formed between peptide:N-glycanase and Rad23p exhibits enhanced deglycosylation activity, which suggests an important role for this enzyme in the misfolded glycoprotein degradation pathway in vivo
physiological function
-
the complex formed between peptide:N-glycanase and Rad23p exhibits enhanced deglycosylation activity, which suggests an important role for this enzyme in the misfolded glycoprotein degradation pathway in vivo
physiological function
-
the peptide:N-glycanase ortholog PNG1 is essential for cell polarity despite its lack of enzymatic activity, PNG1 is involved in cell wall integrity
physiological function
-
the enzyme is a deglycosylating enzyme involved in the endoplasmic reticulum-associated degradation process
physiological function
the enzyme is involved in a different de-N-glycosylation mechanism associated with plant growth and development
physiological function
-
the enzyme plays a critical role during larval development and metamorphosis
physiological function
the N-terminal domain of PNGase (PUB) serves as a possible activator of HR23 in endoplasmic reticulum-associated degradation mechanisms
physiological function
the enzyme is an essential protein, important in aggregation during multicellular development of the organism
physiological function
Fbs1, a glycoprotein-specific ubiquitin ligase, protects misfolded glycoproteins from the action of cytoplasmic PNGase
physiological function
Fbs1, a glycoprotein-specific ubiquitin ligase, protects misfolded glycoproteins from the action of cytoplasmic PNGase
physiological function
PNGase F-II might have a function distinct from that of PNGase F
physiological function
the enzyme hydrolyzes the beta-aspartyl-glycosylamine bond of N-linked glycopeptides, and is involved in the degradation of misfolded or function-lost glycoproteins. cPNGase is believed to be involved in the protein quality control system, while aPNGase is involved in the release of N-glycan units from various glycopeptides produced in the degradation process of function-lost or aged glycoproteins
physiological function
the enzyme hydrolyzes the beta-aspartyl-glycosylamine bond of N-linked glycopeptides, and is involved in the degradation of misfolded or function-lost glycoproteins. cPNGase is believed to be involved in the protein quality control system, while aPNGase is involved in the release of N-glycan units from various glycopeptides produced in the degradation process of function-lost or aged glycoproteins
physiological function
the enzyme hydrolyzes the beta-aspartyl-glycosylamine bond of N-linked glycopeptides, and is involved in the degradation of misfolded or function-lost glycoproteins. cPNGase is believed to be involved in the protein quality control system, while aPNGase is involved in the release of N-glycan units from various glycopeptides produced in the degradation process of function-lost or aged glycoproteins
physiological function
-
the enzyme hydrolyzes the beta-aspartyl-glycosylamine bond of N-linked glycopeptides, and is involved in the degradation of misfolded or function-lost glycoproteins. cPNGase is believed to be involved in the protein quality control system, while aPNGase is involved in the release of N-glycan units from various glycopeptides produced in the degradation process of function-lost or aged glycoproteins
-
physiological function
Dictyostelium discoideum NC-4 / ATCC 24697
-
the enzyme is an essential protein, important in aggregation during multicellular development of the organism
-
physiological function
-
the enzyme hydrolyzes the beta-aspartyl-glycosylamine bond of N-linked glycopeptides, and is involved in the degradation of misfolded or function-lost glycoproteins. cPNGase is believed to be involved in the protein quality control system, while aPNGase is involved in the release of N-glycan units from various glycopeptides produced in the degradation process of function-lost or aged glycoproteins
-
additional information
DdPNGase possess the catalytic triad residues Cys210, His237 and Asp252. DdPNGase also possess the corresponding Trp239 and Trp248, Arg229 and Glu241 conserved residues which possibly are essential for catalysis, structure homology modeling, overview
additional information
-
DdPNGase possess the catalytic triad residues Cys210, His237 and Asp252. DdPNGase also possess the corresponding Trp239 and Trp248, Arg229 and Glu241 conserved residues which possibly are essential for catalysis, structure homology modeling, overview
additional information
structural comparison with PNGase F reveals a relatively larger glycan-binding groove in the catalytic domain and an additional bowl-like domain at the N-terminus of the protein
additional information
-
structural comparison with PNGase F reveals a relatively larger glycan-binding groove in the catalytic domain and an additional bowl-like domain at the N-terminus of the protein
additional information
Dictyostelium discoideum NC-4 / ATCC 24697
-
DdPNGase possess the catalytic triad residues Cys210, His237 and Asp252. DdPNGase also possess the corresponding Trp239 and Trp248, Arg229 and Glu241 conserved residues which possibly are essential for catalysis, structure homology modeling, overview
-
Show AA Sequence and Transmembrane Helices (1422 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105000
-
2 * 105000, homodimer, SDS-PAGE, 41% content of hydrophobic acids
27000
Prunus amygdalus var. dulcis
-
1 * 55000 + 1 * 27000, SDS-PAGE and two-dimensional electrophoresis
34700
-
1 * 34700, native enzyme, 314 amino acid open reading frame
55000
Prunus amygdalus var. dulcis
-
1 * 55000 + 1 * 27000, SDS-PAGE and two-dimensional electrophoresis
70000
-
x * 70000, recombinant enzyme, SDS-PAGE, x 61500, about, sequence calculation
79500
-
estimation by HPLC, from a standard curve of proteins of known molecular mass
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
?
-
x * 70000, recombinant enzyme, SDS-PAGE, x 61500, about, sequence calculation
?
-
x * 70000, recombinant enzyme, SDS-PAGE, x 61500, about, sequence calculation
-
dimer
-
537 amino acids, 59335 Da-translation product, about 70000 Da after processing, dissociation in SDS leads to heterodimer, cleaving between Thr 335 and Thr 336
dimer
-
2 * 105000, homodimer, SDS-PAGE, 41% content of hydrophobic acids
dimer
Prunus amygdalus var. dulcis
-
1 * 55000 + 1 * 27000, SDS-PAGE and two-dimensional electrophoresis
monomer
-
1 * 34700, native enzyme, 314 amino acid open reading frame
additional information
domain organization and tertiary structure modeling, overview
additional information
-
domain organization and tertiary structure modeling, overview
additional information
Dictyostelium discoideum NC-4 / ATCC 24697
-
domain organization and tertiary structure modeling, overview
-
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
additional information
-
enzyme domain structure and enzyme-HR23 complex structure analysis, the enzyme contains a catalytic transglutaminase-like fold, a catalytic cleft structure, a zinc binding domain, and an XPCB association motif, overview
additional information
-
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
additional information
-
enzyme-Rad23 interaction and complex formation analysis, the UBA domain of Rad23 is required, rad mutant does not interact with the enzyme, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
no glycoprotein
glycoprotein
-
59335 primary translation product + 9 to 11 posttranscriptional added high mannose chains, average Man5GlcNAc2
glycoprotein
the enzyme possesses 10 N-glycosylation sites at positions of 220, 266, 386, 397, 447, 481, 489, 551, 556 and 570 in the deduced polypeptide chain
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified His6-tagged wild-type and selenomethionine-labeled enzymes, hanging drop vapor diffusion method, method optimization, SeMet-labeled enzyme from 10% PEG 4000, 0.01 M MgCl2, 0.2 M KCl, and 0.05 M sodium cacodylate, pH 6.5, and native PNGase F-II crystals from 12% PEG 3350 and 0.1 M sodium malonate, pH 7.0, 16ĆĀ°C, X-ray diffraction structure determination and analysis at 2.8 A and 1.9 A resolution, respectively, molecular replacement using the structure of native PNGase F-II as the search model
purified wild-type PUB domain, also as selenomethionine variants, by sitting drop vapour diffusion method at 17ĆĀ°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
-
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
-
the crystal structure of PNGase in complex with N,N'-diacetylchitobiose is described, refined at 3.4 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C251A
-
the mutant exhibits a defect in degrading RTADELTA-transmembrane-Leu2 protein. Expression of the catalytic mutant results in significant stabilization of RTADELTA protein by binding to N-glycans on the substrate
L66M/L75M/L87M
-
site-directed mutagenesis, the PUB domain mutant shows slightly reduced p97 binding
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
C191A
D235A
H218A
H218Y
-
site-directed mutagenesis, the mutant is inactive in protein glycosylation, but interacts with protein Rad23
Q239A
mutation near the nonreducing end of the chitobiose, possible mannose binding site
Q243A
mutation near the nonreducing end of the chitobiose, possible mannose binding site
additional information
C191A
-
site-directed mutagenesis, inactive mutant, inhibitor Z-VAD-fmk does not bind to the mutant enzyme
C191A
-
mutant enzyme does not bind to the inhibitor Man9GlcNAc2-iodoacetoamide
additional information
generation of a At3g14920 gene knockout mutant, complete deletion of aPNGase activity in F1 self plants, screened for At3g14920/At5g05480 double-knockout, from Arabidopsis Columbia T-DNA insertion mutant lines SALK_011366 (At3g14920) and SALK_018420 (At5g05480)
additional information
generation of a At3g14920 gene knockout mutant, complete deletion of aPNGase activity in F1 self plants, screened for At3g14920/At5g05480 double-knockout, from Arabidopsis Columbia T-DNA insertion mutant lines SALK_011366 (At3g14920) and SALK_018420 (At5g05480)
additional information
generation of a At5g05480 gene knockout mutant, complete deletion of aPNGase activity in F1 self plants, screened for At3g14920/At5g05480 double-knockout, from Arabidopsis Columbia T-DNA insertion mutant lines SALK_011366 (At3g14920) and SALK_018420 (At5g05480)
additional information
generation of a At5g05480 gene knockout mutant, complete deletion of aPNGase activity in F1 self plants, screened for At3g14920/At5g05480 double-knockout, from Arabidopsis Columbia T-DNA insertion mutant lines SALK_011366 (At3g14920) and SALK_018420 (At5g05480)
additional information
-
generation of a At5g05480 gene knockout mutant, complete deletion of aPNGase activity in F1 self plants, screened for At3g14920/At5g05480 double-knockout, from Arabidopsis Columbia T-DNA insertion mutant lines SALK_011366 (At3g14920) and SALK_018420 (At5g05480)
-
additional information
-
generation of a At3g14920 gene knockout mutant, complete deletion of aPNGase activity in F1 self plants, screened for At3g14920/At5g05480 double-knockout, from Arabidopsis Columbia T-DNA insertion mutant lines SALK_011366 (At3g14920) and SALK_018420 (At5g05480)
-
additional information
generation of a Ddpngase gene disruption construct, a png-/Ax2 knockout strain, knockout mutants show defect in aggregation
additional information
-
generation of a Ddpngase gene disruption construct, a png-/Ax2 knockout strain, knockout mutants show defect in aggregation
additional information
Dictyostelium discoideum NC-4 / ATCC 24697
-
generation of a Ddpngase gene disruption construct, a png-/Ax2 knockout strain, knockout mutants show defect in aggregation
-
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
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
additional information
-
enzyme deletion strain, formation of free oligosaccharides is reduced by 70-80%
additional information
-
site-directed mutagenesis of not conserved amino acids
additional information
-
deletion of the N-terminal H1 helix (Png1p-DH1) enhances the deglycosylation activity of peptide:N-glycanase towards denatured glycoproteins
additional information
-
deletion of the N-terminal H1 helix (Png1p-DH1) enhances the deglycosylation activity of peptide:N-glycanase towards denatured glycoproteins
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
stable up to 24 h, unstable at temperatures above 30ĆĀ°C after 1-3 h
37
37 - 45
-
Png1p is inactive at 37ĆĀ°C. In contrast, the Png1p-Rad23p complex still possesses enzymatic activity at 45ĆĀ°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the recombinantly expressed enzyme is rapidly degraded after Escherichia coli cell lysis in Tris/HCl buffer which is commonly used in cell disruption procedures, although a protease inhibitor is added
-
zinc binding stabilizes the enzyme conformation by stabilizing the intermediate state and promoting product release
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme by Fe2+ affinity and phosphopeptide affinity chromatography to over 95% purity
-
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
-
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
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinit chromatography
-
recombinant His-tagged enzyme PNGase Yl from Pichia pastoris strain GS115 by ultracentrifugatio, dialysis, and nickel affinity chromatography
-
recombinant His6-tagged wild-type and selenomethionine-labeled enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration
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
-
recombinant wild-type and mutant Png1 from Escherichia coli strain BL21(DE3)
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
co-expression of His6-tagged full-length enzyme or truncated versions with full-length Rad23 Escherichia coli strain BL21(DE3)
-
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
-
DNA and amino acid sequence determination and analysis, recombinant expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli strain JM109 and in Pichia pastoris strain GS115
expression in Escherichia coli
expression of HA-tagged wild-type and mutant enzymes in U373 astrocytoma cells
-
expression of His- or FLAG-tagged wild-type and mutant enzymes, co-expression with Rad23
-
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)
-
gene DDB0189828, sequence comparisons and phylogenetic analysis
gene Ddpngase, single copy gene, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression under control of the constitutive promoter actin 15 and fused to enhanced yellow fluorescent protein (EYFP), in the mutant axenic strain Ax2
gene NGLY1, sequence comparisons and phylogenetic analysis
gene png1, expression of wild-type and mutant Png1 in Escherichia coli strain BL21(DE3)
-
gene PNG1, sequence comparisons and phylogenetic analysis
gene PNGase F-II, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of His6-tagged wild-type and selenomethionine-labeled enzyme in Escherichia coli strain BL21(DE3)
importantly, heterologous expression of AtPNG1 restores N-glycanase activity in a PNGase-deficient Saccharomyces cerevisiae mutant
-
into the vector pET28a for expression in Escherichia coli BL21DE3 Codon Plus RIL cells
overexpression of the full-length enzyme, enzyme core domain, and enzyme XPCB domain in Escherichia coli strain BL21(DE3)
-
PNGase Yl, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Pichia pastoris strain GS115
-
recombinant expression in an Arabidopsis thaliana aPNGase-knockout line
the PNGase F gene from Flavobacterium meningosepticum is cloned into plasmid pYD1, which enables regulated expression, secretion and detection. The expression of PNGase F gene at extracellular surface of Saccharomyces cerevisiae is confirmed by immunofluorescence microscopy. Fluorescence activated cell sorter analysis indicates that, after 36 h cultivation, 47.6% of the cell surface is anchored with target proteins. The surface engineered enzyme is confirmed to be active and reached its highest level after induced for 36 h
-
recombinant expression in an Arabidopsis thaliana aPNGase-knockout line
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
synthesis
-
PNGase F can be utilized for glycosylation of non-glycosylated recombinant proteins produced in prokaryotic cells
analysis
-
valuable tool to characterize the peptide portion of glycoproteins and glycopeptides to release asparagine-linked oligosaccarides for structural analysis, recombinant PNGase F contains no contaminant Endo F, proteases or exoglycosidases
analysis
-
a procedure to map N-glycosylation sites is presented, it can be applied to purified proteins as well as to highly complex mixtures. The method exploits deglycosylation by PNGase F in a diagonal, reverse-phase chromatographic setup
analysis
-
the facile expression, non-glycosylated nature, unusual pH optimum and broad substrate specificity of the enzyme makes recombinant PNGase H+ a versatile tool in N-glycan analysis
analysis
-
the facile expression, non-glycosylated nature, unusual pH optimum and broad substrate specificity of the enzyme makes recombinant PNGase H+ a versatile tool in N-glycan analysis
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tarentino, A.L.; Plummer, T.H.
Peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase and endo-beta-N-acetylglucosaminidase from Flavobacterium meningosepticum
Methods Enzymol.
138
770-778
1987
Elizabethkingia meningoseptica
brenda
Makino, M.; Kojima, T.; Ohgushi, T.; Yamashina, I.
Studies on enzymes acting on glycopeptides
J. Biochem.
63
186-192
1968
Cavia porcellus, Rattus norvegicus, Sus scrofa
brenda
Takahashi, N.
Demonstration of a new amidase acting on glycopeptides
Biochem. Biophys. Res. Commun.
76
1194-1201
1977
Prunus amygdalus var. dulcis
brenda
Takahashi, N.; Nishibe, H.
Some characteristics of a new glycopeptidase acting on aspartylglycosylamine linkages
J. Biochem.
84
1467-1473
1978
Prunus amygdalus var. dulcis
brenda
Ishihara, H.; Takahashi, N.; Oguri, S.; Tejima, S.
Complete structure of the carbohydrate moiety of stem bromelain. An application of the almond glycopeptidase for structural studies of glycopeptides
J. Biol. Chem.
254
10715-10719
1979
Prunus amygdalus var. dulcis
brenda
Takahashi, N.; Nishibe, H.
Almond glycopeptidase acting on aspartylglycosylamine linkages. Multiplicity and substrate specificity
Biochim. Biophys. Acta
657
457-467
1981
Prunus amygdalus var. dulcis
brenda
Nishibe, H.; Takahashi, N.
The release of carbohydrate moieties from human fibrinogen by almond glycopeptidase without alteration in fibrinogen clottability
Biochim. Biophys. Acta
661
274-279
1981
Prunus amygdalus var. dulcis
brenda
Takahashi, N.; Shimizu, S.; Yamada, K.
Asparagine-linked oligosaccharides in human placenta and umbilical cord as demonstrated by almond glycopeptidase
FEBS Lett.
146
139-142
1982
Prunus amygdalus var. dulcis
brenda
Takahashi, N.; Toda, H.; Nishibe, H.; Yamamoto, K.
Isolation and characterization of Taka-amylase A apoprotein deglycosylated by digestion with almond glycopeptidase immobilized on Sepharose
Biochim. Biophys. Acta
707
236-242
1982
Prunus amygdalus var. dulcis
brenda
Sugiyama, K.; Ishihara, H.; Tejima, S.; Takahashi, N.
Demonstration of a new glycopeptidase, from jack-bean meal, acting on aspartylglucosylamine linkages
Biochem. Biophys. Res. Commun.
112
155-160
1983
Canavalia ensiformis
brenda
Tomiya, N.; Kurono, M.; Ishihara, H.; Tejima, S.; Endo, S.; Arata, Y.; Takahashi, N.
Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography
Anal. Biochem.
163
489-499
1987
Canavalia ensiformis
brenda
Plummer Jr., T.H.; Phelan, A.W.; Tarentino, A.L.
Detection and quantification of peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidases
Eur. J. Biochem.
163
167-173
1987
Canavalia ensiformis, Lens culinaris, Pisum sativum, Prunus amygdalus var. dulcis, Triticum aestivum
brenda
Barsomian, G.D.; Johnson, T.L.; Borowski, M.; Denman, J.; Ollington, J.F.; Hirani, S.; McNeilly, D.S.; Rasmussen, J.R.
Cloning and expression of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F in Escherichia coli
J. Biol. Chem.
265
6967-6872
1990
Elizabethkingia meningoseptica
brenda
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
Kuhn, P.; Tarentino, A.L.; Plummer, T.H.; Van Roey, P.
Crystal structure of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F at 2.2-A resolution
Biochemistry
33
11699-11706
1994
Elizabethkingia meningoseptica
brenda
Lhernould, S.; Karamanos, Y.; Lerouge, P.; Morvan, H.
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