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acetylcholine receptor + H2O
?
-
-
-
-
?
alpha-dansyl derivative fetuin pentaglycopeptide + H2O
?
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
-
-
?
asialo fetuin glycopeptide I + H2O
?
-
-
-
-
?
asialoglycopeptide I + H2O
?
-
fetuin-derived radio-labeled substrate, deglycosylation
-
-
?
asiolo-ovomucoid glycopeptide + H2O
?
-
-
-
-
?
bence-jones wh lambda glycopeptide + H2O
?
-
acid PNGase M from blastoderm stage 11
-
-
?
beta-aspartylglycosylamine + H2O
aspartic acid + NH3 + N-acetylglucosamine
bovine fetuin glycopeptide + H2O
?
bromelain glycopeptide + H2O
?
Prunus amygdalus var. dulcis
-
-
-
-
?
bromelain undecapeptide + H2O
?
Prunus amygdalus var. dulcis
-
-
-
-
?
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
dEDANSylated hen ovomucoid glycopeptide + H2O
?
denatured ribonuclease B + H2O
?
-
-
-
-
?
denatured RNase B + H2O
?
-
SpPNGase cleaves N-glycan from denatured RNase B
-
-
?
denatured RNaseB + H2O
deglycosylated RNaseB
-
-
-
?
fetuin glycopeptide + H2O
?
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
-
-
?
Gal2GlcNAc2Man3GlcNAc2-Asn-peptide + H2O
?
-
-
-
-
?
GlcNAc-Asn-peptide + H2O
?
-
-
-
-
?
glycoprotein US11 + H2O
?
-
the enzyme deglycolyzes HCMV glycoprotein US11
-
-
?
glycoprotein US2 + H2O
?
-
the enzyme deglycolyzes HCMV glycoprotein US2
-
-
?
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
-
-
?
human asialotransferrin + H2O
?
-
-
-
-
?
human IgG + H2O
?
-
-
-
-
?
human transferrin glycopeptide + H2O
?
-
-
-
?
L-hyosophorin + H2O
?
-
neutral and acid PNGase M
-
-
?
laccase + H2O
?
-
-
-
-
?
Leu-Asn(GlcNAc5Man3Gal3)-Asp-Ser-Arg + H2O
?
fetuin-derived asialoglycopeptide I, 14C, substrate activity assay
-
-
?
Man5GlcNAc2-Asn-peptide + H2O
?
-
-
-
-
?
melanopsin + H2O
?
-
-
-
?
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
-
-
?
ovalbumin glycopeptide + H2O
aspartic acid + NH3 + N-acetylglucosamine
ovotransferrin glycopeptide + H2O
?
Prunus amygdalus var. dulcis
-
Gly-Leu-Ile-His-Asn(oligosaccharide)-Arg
-
-
?
PHA glycopeptide + H2O
?
-
-
-
-
?
pineapple stem bromelain glycopeptide + H2O
?
porcine fibrinogen + H2O
?
-
-
-
-
?
proton-coupled folate transporter + H2O
?
-
-
-
-
?
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
-
-
?
transferrin + H2O
?
Prunus amygdalus var. dulcis
-
desialylated, human
-
-
?
truncated RNaseB + H2O
deglycosylated RNaseB
-
-
-
?
XylMan3FucGlcNAc2-Asn-peptide from horse raddish peroxidase + H2O
?
-
-
-
-
?
yeast carboxypeptidase + H2O
?
-
deglycosylation of heat-denatured protein
-
-
?
additional information
?
-
alpha-dansyl derivative fetuin pentaglycopeptide + H2O
?
-
-
-
-
?
alpha-dansyl derivative fetuin pentaglycopeptide + H2O
?
-
-
-
-
?
alpha-dansyl derivative fetuin pentaglycopeptide + H2O
?
-
-
-
-
?
alpha-dansyl derivative fetuin pentaglycopeptide + H2O
?
Prunus amygdalus var. dulcis
-
-
-
-
?
alpha-dansyl derivative fetuin pentaglycopeptide + H2O
?
-
-
-
-
?
ATPase p97 + H2O
?
a cofactor-binding motif of p97 contained within the last 10 amino acid residues of the C terminus is both necessary and sufficient to mediate interactions of p97 with PNGase. Phosphorylation of p97s highly conserved penultimate tyrosine residue, which is the main phosphorylation site during T cell receptor stimulation, completely blocks binding of either PNGase or Ufd3 to p97. This observation suggests that phosphorylation of this residue modulates endoplasmic reticulum-associated protein degradation activity by discharging substrate-processing cofactors
-
-
?
ATPase p97 + H2O
?
a cofactor-binding motif of p97 contained within the last 10 amino acid residues of the C terminus is both necessary and sufficient to mediate interactions of p97 with PNGase
-
-
?
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
?
-
-
-
-
?
bovine fetuin glycopeptide + H2O
?
-
-
-
-
?
bovine fetuin glycopeptide + H2O
?
-
Leu-Ala-Asn-(oligosaccharide)-AeCys-Ser
-
-
?
bovine fetuin glycopeptide + H2O
?
-
-
-
-
?
bovine fetuin glycopeptide + H2O
?
-
Leu-Asn(Man3Gal3GlcNAc5)-Asp-Ser-Arg
-
-
?
bovine fetuin glycopeptide + H2O
?
-
-
-
-
?
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
-
-
-
-
?
dEDANSylated hen ovomucoid glycopeptide + H2O
?
-
-
-
-
?
dEDANSylated hen ovomucoid glycopeptide + H2O
?
-
DGP
-
-
?
fetuin glycopeptide + H2O
?
-
-
-
-
?
fetuin glycopeptide + H2O
?
-
-
-
-
?
fetuin glycopeptide + H2O
?
Prunus amygdalus var. dulcis
-
-
-
-
?
glycopeptide + H2O
?
Prunus amygdalus var. dulcis
-
with 3-11 amino acid residues
-
-
?
glycopeptide + H2O
?
-
-
-
-
?
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 60-65ºC or by 40-60 mM dithiothreitol, its deglycosylation by Png1p is most prominent
-
-
?
RNase B + H2O
?
-
-
-
-
?
RNase B + H2O
?
-
-
-
-
?
RNase B + H2O
?
-
the enzyme deglycolyzes RNaseB
-
-
?
RNase B + H2O
?
-
-
-
-
?
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
?
-
-
-
-
-
?
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
?
-
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
?
-
-
-
-
-
?
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
?
-
Prunus amygdalus var. dulcis
-
-
-
-
?
additional information
?
-
Prunus amygdalus var. dulcis
-
-
-
-
?
additional information
?
-
Prunus amygdalus var. dulcis
-
-
-
-
?
additional information
?
-
Prunus amygdalus var. dulcis
-
-
-
-
?
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
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
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
?
-
-
-
-
-
?
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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2-mercaptoethanol
-
20% inhibition at 100 mM
benzyloxycarbonyl-VAD-fluoromethyl ketone
-
-
benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone
-
covalently bind to the active site Cys191 of recombinant yeast peptide N-glycanase
Ca2+
2 mM, 19% inhibition
carbobenzyloxy-Val-Ala-Asp
carbobenzyloxy-Val-Ala-Asp-alpha-fluoromethylketone
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
-
Fe2+
2 mM, 90% inhibition
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
-
K+
-
significant inactivation by 100 mM
L-hyosphorin derived nonapeptide
-
1 mM causes 92% inbition of acid PNGase M
-
liberated glycan reaction product
-
Man8GlcNAc2-iodoacetoamide
-
-
Man9GlcNAc2-iodoacetoamide
-
strong inhibitor, irreversibly inhibits that catalytic Cys in a highly specific manner
Mg2+
2 mM, 14% inhibition
N,N'-diacetylchitobiosylbromoacetamide
-
-
N,N'-diacetylchitobiosylchloroacetamide
-
-
N,N'-diacetylchitobiosyliodoacetamide
-
-
N-benzyloxycarbonyl-VAD-fluoromethylketone
Z-VAD-fmk
Na+
-
significant inactivation by 100 mM
p-chloromercuribenzoic acid
-
0.5 mM causes 89% inhibition of neutral PNGase M
phosphate buffers
-
no significant activity
-
SDS
-
complete inactivation by 0.05% SDS can be corrected by the addition of 1% Nonidet P-40
Tris-HCl
-
no significant activity
Triton X100
-
40% inhibition at 1%
Urea
-
80% inhibition at 2 M
ZnCl2
-
10-20% remaining activity at neutral PNGase M by 5 mM
carbobenzyloxy-Val-Ala-Asp
-
i.e. Z-VAD, in vivo inhibition
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
-
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
Co2+
2 mM, almost complete inhibition
Co2+
-
28% remaining activity by 2 mM
Cu2+
2 mM, almost complete inhibition
Cu2+
-
partial inhibition
Cu2+
Prunus amygdalus var. dulcis
-
-
EDTA
-
23% inhibition by 5 mM, 13% inhibition by 10 mM
EDTA
-
activity is not restored by adding metal ions
EDTA
-
not restored by readdition of metal ions
Fe3+
-
-
Fe3+
Prunus amygdalus var. dulcis
-
-
Glycoasparagine
-
1 mM causes 86% inhibition
liberated glycan reaction product
-
causes 82% inhibition
-
liberated glycan reaction product
-
-
-
Mn2+
2 mM, 56% inhibition
Mn2+
-
33% remaining activity by 2 mM
Monoiodoacetic acid
-
2 mM causes 64% inhibition
Monoiodoacetic acid
-
2 mM, significant inhibition by thiol-modification
Monoiodoacetic acid
-
5 mM causes 82% inhibition of the neutral PNGase M
N,N'-diacetylchitobiose
-
-
N,N'-diacetylchitobiose
-
GlcNAc2, competitive inhibitor may be directly accessible to the catalytic site
N,N'-diacetylchitobiose
Prunus amygdalus var. dulcis
-
-
N-ethylmaleimide
-
2 mM, significant inhibition by thiol-modification, alkylation
N-ethylmaleimide
-
5 mM causes complete inhibition
triomannose
-
-
triomannose
-
evidence for occupation of the carbohydrate-binding site
Z-VAD-fmk
-
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
Zn2+
2 mM, almost complete inhibition
Zn2+
Prunus amygdalus var. dulcis
-
-
Zn2+
-
51% remaining activity by 2 mM
additional information
-
no effect: yeast mannan, trimannose
-
additional information
-
no inhibition by the caspase inhibitor Q-VD-OPh
-
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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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
-
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
-
PNG1 deletion results in strong polarity defects
malfunction
-
homozygous deletion mutants show developmental defect
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
-
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
-
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
-
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
-
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
-
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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.
Characterization of the peptide-N4-(N-acetylglucosaminyl)asparagine amidase (PNGase Se) from Silene alba cells
Glycoconj. J.
12
94-98
1995
Silene latifolia subsp. alba
brenda
Kitajima, K.; Suzuki, T.; Kouchi, Z.; Inoue, S.; Inoue, Y.
Identification and distribution of peptide:N-glycanase (PNGase) in mouse organs
Arch. Biochem. Biophys.
319
393-401
1995
Mus musculus
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Suzuki, T.; Kitajima, K.; Inoue, Y.; Inoue, S.
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Elizabethkingia meningoseptica
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Elizabethkingia meningoseptica
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Saccharomyces cerevisiae
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Rattus norvegicus (Q5XI55)
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Unal, E.S.; Zhao, R.; Qiu, A.; Goldman, I.D.
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Homo sapiens
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Saccharomyces cerevisiae (Q02890), Saccharomyces cerevisiae
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Saccharomyces cerevisiae, Elizabethkingia meningoseptica, Schizosaccharomyces pombe
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Homo sapiens
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Elizabethkingia meningoseptica
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Arabidopsis thaliana
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Mus musculus (Q9JI78)
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Solanum lycopersicum (D0QU16), Solanum lycopersicum
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Evidence for an essential deglycosylation-independent activity of PNGase in Drosophila melanogaster
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Saccharomyces cerevisiae, Drosophila melanogaster
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Wang, T.; Cai, Z.P.; Gu, X.Q.; Ma, H.Y.; Du, Y.M.; Huang, K.; Voglmeir, J.; Liu, L.
Discovery and characterization of a novel extremely acidic bacterial N-glycanase with combined advantages of PNGase F and A
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Terriglobus roseus, Terriglobus roseus DSM 18391
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Gosain, A.; Lohia, R.; Shrivastava, A.; Saran, S.
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Dictyostelium discoideum (Q55FC8), Dictyostelium discoideum, Dictyostelium discoideum NC-4 / ATCC 24697 (Q55FC8)
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Lee, K.J.; Gil, J.Y.; Kim, S.Y.; Kwon, O.; Ko, K.; Kim, D.I.; Kim, D.K.; Kim, H.H.; Oh, D.B.
Molecular characterization of acidic peptide:N-glycanase from the dimorphic yeast Yarrowia lipolytica
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Yarrowia lipolytica, Yarrowia lipolytica SMS397A
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Uemura, R.; Ogura, M.; Matsumaru, C.; Akiyama, T.; Maeda, M.; Kimura, Y.
Novel assay system for acidic peptide N-glycanase (aPNGase) activity in crude plant extract
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Solanum lycopersicum (F8QR42), Prunus dulcis (P81898), Arabidopsis thaliana (Q9FFG6), Arabidopsis thaliana (Q9LKB2), Solanum lycopersicum Micro-Tom (F8QR42), Arabidopsis thaliana Col-0 (Q9FFG6), Arabidopsis thaliana Col-0 (Q9LKB2)
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Suzuki, T.
The cytoplasmic peptide N-glycanase (Ngly1) - basic science encounters a human genetic disorder
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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)
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Sun, G.; Yu, X.; Bao, C.; Wang, L.; Li, M.; Gan, J.; Qu, D.; Ma, J.; Chen, L.
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Elizabethkingia meningoseptica (A0A090KI56), Elizabethkingia meningoseptica
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