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Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC 3.5.1.52) (Peptide:N-glycanase) (PNGase)

 NGLY1_CAEEL             Reviewed;         606 AA.
Q9TW67; Q9NBD6;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
16-JAN-2019, entry version 146.
RecName: Full=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase;
EC=3.5.1.52;
AltName: Full=Peptide:N-glycanase;
Short=PNGase;
Name=png-1; ORFNames=F56G4.5;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 65-606.
PubMed=10831608; DOI=10.1083/jcb.149.5.1039;
Suzuki T., Park H., Hollingsworth N.M., Sternglanz R., Lennarz W.J.;
"PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase.";
J. Cell Biol. 149:1039-1052(2000).
[3]
FUNCTION, AND MUTAGENESIS OF CYS-251.
PubMed=17509531; DOI=10.1016/j.bbrc.2007.04.199;
Suzuki T., Tanabe K., Hara I., Taniguchi N., Colavita A.;
"Dual enzymatic properties of the cytoplasmic peptide: N-glycanase in
C. elegans.";
Biochem. Biophys. Res. Commun. 358:837-841(2007).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
PubMed=17522090; DOI=10.1093/jb/mvm117;
Kato T., Kawahara A., Ashida H., Yamamoto K.;
"Unique peptide:N-glycanase of Caenorhabditis elegans has activity of
protein disulphide reductase as well as of deglycosylation.";
J. Biochem. 142:175-181(2007).
[5]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-498.
PubMed=27528192; DOI=10.7554/eLife.17721;
Lehrbach N.J., Ruvkun G.;
"Proteasome dysfunction triggers activation of SKN-1A/Nrf1 by the
aspartic protease DDI-1.";
Elife 5:0-0(2016).
-!- FUNCTION: Specifically deglycosylates the denatured form of N-
linked glycoproteins in the cytoplasm and assists their
proteasome-mediated degradation (PubMed:17509531,
PubMed:17522090). Cleaves the beta-aspartyl-glucosamine (GlcNAc)
of the glycan and the amide side chain of Asn, converting Asn to
Asp (PubMed:17522090). Prefers proteins containing high-mannose
over those bearing complex type oligosaccharides
(PubMed:17522090). Can recognize misfolded proteins in the
endoplasmic reticulum that are exported to the cytosol to be
destroyed and deglycosylate them, while it has no activity toward
native proteins (PubMed:17509531). Deglycosylation is a
prerequisite for subsequent proteasome-mediated degradation of
some, but not all, misfolded glycoproteins (PubMed:17509531). Also
displays oxidoreductase (thioredoxin) activity (PubMed:17509531,
PubMed:17522090). Involved in regulating the expression of
proteasomal subunits such as rpt-3 in order to confer resistance
to proteasomal dysfunction (PubMed:27528192).
{ECO:0000269|PubMed:17509531, ECO:0000269|PubMed:17522090,
ECO:0000269|PubMed:27528192}.
-!- CATALYTIC ACTIVITY:
Reaction=Hydrolysis of an N(4)-(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.; EC=3.5.1.52;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- ACTIVITY REGULATION: Inhibited by Zn(2+) and z-VAD-fmk (caspase
inhibitor) but unaffected by EDTA. {ECO:0000269|PubMed:17522090}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17522090}.
Endoplasmic reticulum {ECO:0000269|PubMed:17522090}. Note=ER
localization inferred from partial colocalization with an ER
marker, membrane protein PIG-X.
-!- DISRUPTION PHENOTYPE: Double knockout with rpt-5 RNAi results in
failed expression of the proteasomal subunit rpt-3.
{ECO:0000269|PubMed:27528192}.
-!- SIMILARITY: Belongs to the transglutaminase-like superfamily.
PNGase family. {ECO:0000255|PROSITE-ProRule:PRU00731}.
-----------------------------------------------------------------------
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EMBL; Z81552; CAB04487.2; -; Genomic_DNA.
EMBL; AL117201; CAB04487.2; JOINED; Genomic_DNA.
EMBL; AF250925; AAF74721.1; -; mRNA.
PIR; E87921; E87921.
PIR; T31557; T31557.
RefSeq; NP_492913.1; NM_060512.4.
UniGene; Cel.18605; -.
ProteinModelPortal; Q9TW67; -.
SMR; Q9TW67; -.
BioGrid; 38436; 2.
DIP; DIP-24462N; -.
IntAct; Q9TW67; 2.
STRING; 6239.F56G4.5.1; -.
EPD; Q9TW67; -.
PaxDb; Q9TW67; -.
PeptideAtlas; Q9TW67; -.
PRIDE; Q9TW67; -.
EnsemblMetazoa; F56G4.5; F56G4.5; WBGene00010160.
GeneID; 173028; -.
KEGG; cel:CELE_F56G4.5; -.
CTD; 173028; -.
WormBase; F56G4.5; CE23786; WBGene00010160; png-1.
eggNOG; KOG0907; Eukaryota.
eggNOG; KOG0909; Eukaryota.
eggNOG; ENOG410XP69; LUCA.
GeneTree; ENSGT00390000006540; -.
InParanoid; Q9TW67; -.
KO; K01456; -.
OMA; VWNEVYL; -.
OrthoDB; 917526at2759; -.
PhylomeDB; Q9TW67; -.
BRENDA; 3.5.1.52; 1045.
Reactome; R-CEL-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
PRO; PR:Q9TW67; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00010160; Expressed in 5 organ(s), highest expression level in material anatomical entity.
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; IDA:WormBase.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IDA:WormBase.
GO; GO:0047134; F:protein-disulfide reductase activity; IDA:WormBase.
GO; GO:0045454; P:cell redox homeostasis; IGI:WormBase.
GO; GO:0006516; P:glycoprotein catabolic process; ISS:UniProtKB.
GO; GO:0048671; P:negative regulation of collateral sprouting; IMP:WormBase.
GO; GO:0006517; P:protein deglycosylation; IDA:WormBase.
GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IGI:WormBase.
Gene3D; 2.60.120.1020; -; 1.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR038680; PAW_sf.
InterPro; IPR006588; Peptide_N_glycanase_PAW_dom.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
InterPro; IPR002931; Transglutaminase-like.
Pfam; PF04721; PAW; 1.
Pfam; PF00085; Thioredoxin; 1.
Pfam; PF01841; Transglut_core; 1.
SMART; SM00613; PAW; 1.
SMART; SM00460; TGc; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF52833; SSF52833; 1.
SUPFAM; SSF54001; SSF54001; 1.
PROSITE; PS51398; PAW; 1.
PROSITE; PS00194; THIOREDOXIN_1; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Endoplasmic reticulum; Hydrolase;
Metal-binding; Reference proteome; Zinc.
CHAIN 1 606 Peptide-N(4)-(N-acetyl-beta-
glucosaminyl)asparagine amidase.
/FTId=PRO_0000248978.
DOMAIN 2 108 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 404 606 PAW. {ECO:0000255|PROSITE-
ProRule:PRU00731}.
ACT_SITE 251 251 Nucleophile.
ACT_SITE 278 278 {ECO:0000250}.
ACT_SITE 295 295 {ECO:0000250}.
METAL 191 191 Zinc. {ECO:0000250}.
METAL 194 194 Zinc. {ECO:0000250}.
METAL 225 225 Zinc. {ECO:0000250}.
METAL 228 228 Zinc. {ECO:0000250}.
MUTAGEN 251 251 C->Y: Loss of PNGase activity.
{ECO:0000269|PubMed:17509531}.
MUTAGEN 498 498 G->R: In mg561; defective expression of
the proteasomal subunit rpt-3 in a pbs-5
(proteasomal subunit) mutant background.
{ECO:0000269|PubMed:27528192}.
SEQUENCE 606 AA; 69148 MW; 1D3EA2EBDFB40769 CRC64;
MPVTEVGSLP ELNNILERSD ANRLIIIDFF ANWCGPCRMI SPIFEQFSAE YGNATFLKVN
CDVARDIVQR YNISAMPTFI FLKNRQQVDM VRGANQQAIA EKIRQHYSPT PANPNAASDS
EKRFLEQFVK CSNVPRSYQD EVFKALARSV MPEELVGRAM TEGPRDEKAI LKDLLHWFKT
QFFTWFDRPT CPKCTLKCST DGLQGTPTRE EQKEGGASRV EVYICDGCNT EMRFPRYNNP
AKLLQTRTGR CGEWANCFGL LLAALNLESR FIYDTTDHVW NEVYLLAEQR WCHVDPCENT
MDRPLLYTRG WGKTLGYCIG YGSDHVVDVT WRYIWDSKKL VTQRNEVRQP VFENFLSKLN
SRQAEGQTEP RKRELAVRRV CELMEMMAQE AKNHKIGWEK IGDDLGGRIT GSEEWRRERG
ELGESGPKLL AEPIKLAPPT GPAQNYLEFN YDVITDTYSQ PPEIGFSAQA FELENVQRVE
ETDWNMTYLC RKRGDAPGNI SWHFDLKSLK KSIEKIEIRM AGIQKFEKGK AMAIACLGDS
CMRLPIDCSA LTIEDPKNAE ILKITATLSG GEGAIGFQQA QIFRTELKRG GGARTESFSV
KIWMKN


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Pathways :
WP1001: Peptide GPCRs
WP1117: Peptide GPCRs
WP131: Peptide GPCRs
WP1338: Peptide GPCRs
WP1626: Benzoate degradation via CoA ligation
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WP234: Peptide GPCRs
WP24: Peptide GPCRs
WP771: Peptide GPCRs
WP883: Peptide GPCRs
WP1045: TGF-beta Receptor Signaling Pathway
WP1048: TGF Beta Signaling Pathway
WP105: Fatty Acid Beta Oxidation 2
WP1058: Senescence and Autophagy
WP1061: Fatty Acid Beta Oxidation
WP1106: Keap1-Nrf2
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP113: TGF Beta Signaling Pathway
WP1161: TGF-beta Receptor Signaling Pathway
WP1164: TGF Beta Signaling Pathway
WP1177: Fatty Acid Beta Oxidation
WP1207: Fatty Acid Beta Oxidation
WP1224: EBV LMP1 signaling
WP1225: estrogen signalling
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation

Related Genes :
[png-1 F56G4.5] Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC 3.5.1.52) (Peptide:N-glycanase) (PNGase)
[Ngly1] Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (PNGase) (mPNGase) (EC 3.5.1.52) (N-glycanase 1) (Peptide:N-glycanase)
[NGLY1 PNG1] Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (PNGase) (hPNGase) (EC 3.5.1.52) (N-glycanase 1) (Peptide:N-glycanase)
[PNG1 YPL096W] Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (PNGase) (EC 3.5.1.52) (Peptide:N-glycanase 1) (yPNG1)
[ngl png] Peptide-N(4)-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F (PNGase F) (EC 3.5.1.52) (Glycopeptide N-glycosidase) (N-glycanase)
[png1 SPBC1709.14] Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (PNGase) (EC 3.5.1.52) (Peptide:N-glycanase 1)
[Pngl PNGase CG7865] Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC 3.5.1.52) (Peptide:N-glycanase)
[Ngly1] Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (PNGase) (EC 3.5.1.52) (N-glycanase 1) (Peptide:N-glycanase)
[B4galt3] Beta-1,4-galactosyltransferase 3 (Beta-1,4-GalTase 3) (Beta4Gal-T3) (b4Gal-T3) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 3) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 3)
[Gcnt3] Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3 (EC 2.4.1.102) (EC 2.4.1.148) (EC 2.4.1.150) (C2GnT-mucin type) (C2GnT-M) (Mucus-type core 2 beta-1,6-N-acetylglucosaminyltransferase)
[Oga Hexc Kiaa0679 Mgea5] Protein O-GlcNAcase (OGA) (EC 3.2.1.169) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase) (Bifunctional protein NCOAT) (Meningioma-expressed antigen 5) (N-acetyl-beta-D-glucosaminidase) (N-acetyl-beta-glucosaminidase)
[B3GNT3 B3GALT8 TMEM3 UNQ637/PRO1266] N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3 (EC 2.4.1.149) (Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase) (EC 2.4.1.146) (Beta-1,3-galactosyltransferase 8) (Beta-1,3-GalTase 8) (Beta3Gal-T8) (Beta3GalT8) (b3Gal-T8) (Beta-3-Gx-T8) (Core 1 extending beta-1,3-N-acetylglucosaminyltransferase) (Core1-beta3GlcNAcT) (Transmembrane protein 3) (UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 8) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3) (BGnT-3) (Beta-1,3-Gn-T3) (Beta-1,3-N-acetylglucosaminyltransferase 3) (Beta3Gn-T3) (UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 8)
[St3gal3 Siat3 Siat6] CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase (EC 2.4.99.6) (Beta-galactoside alpha-2,3-sialyltransferase 3) (Alpha 2,3-ST 3) (Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase) (N-acetyllactosaminide alpha-2,3-sialyltransferase) (ST3Gal III) (ST3GalIII) (ST3N) (Sialyltransferase 6)
[B3GNT2 B3gnt1 Beta3gnt] N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2 (EC 2.4.1.149) (Beta-1,3-N-acetylglucosaminyltransferase 1) (BGnT-1) (Beta-1,3-Gn-T1) (Beta3Gn-T1) (Beta-1,3-galactosyltransferase 7) (Beta-1,3-GalTase 7) (Beta3Gal-T7) (Beta3GalT7) (b3Gal-T7) (Beta-3-Gx-T7) (UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 7) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2) (BGnT-2) (Beta-1,3-Gn-T2) (Beta-1,3-N-acetylglucosaminyltransferase 2) (Beta3Gn-T2) (UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7)
[NGLY1 QtsA-18143] Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (PNGase) (EC 3.5.1.52) (N-glycanase 1) (Peptide:N-glycanase)
[B3GNT2 B3GALT7 B3GNT1] N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2 (EC 2.4.1.149) (Beta-1,3-N-acetylglucosaminyltransferase 1) (BGnT-1) (Beta-1,3-Gn-T1) (Beta3Gn-T1) (Beta-1,3-galactosyltransferase 7) (Beta-1,3-GalTase 7) (Beta3Gal-T7) (Beta3GalT7) (b3Gal-T7) (Beta-3-Gx-T7) (UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 7) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2) (BGnT-2) (Beta-1,3-Gn-T2) (Beta-1,3-N-acetylglucosaminyltransferase 2) (Beta3Gn-T2) (UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7)
[B4GALT3] Beta-1,4-galactosyltransferase 3 (Beta-1,4-GalTase 3) (Beta4Gal-T3) (b4Gal-T3) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 3) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 3)
[] Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase A (PNGase A) (EC 3.5.1.52) (Glycopeptide N-glycosidase) (N-glycanase) [Cleaved into: Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase A light chain (PNGase A small chain) (PNGase A subunit B); Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase A heavy chain (PNGase A large chain) (PNGase A subunit A)]
[B4GALT1 GGTB2] Beta-1,4-galactosyltransferase 1 (Beta-1,4-GalTase 1) (Beta4Gal-T1) (b4Gal-T1) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (Lactose synthase A protein) (EC 2.4.1.22) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1) [Cleaved into: Processed beta-1,4-galactosyltransferase 1]
[png-1 CBG08042] Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC 3.5.1.52) (Peptide:N-glycanase) (PNGase)
[B4GALT1 GALT GGTB2] Beta-1,4-galactosyltransferase 1 (Beta-1,4-GalTase 1) (Beta4Gal-T1) (b4Gal-T1) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (Lactose synthase A protein) (EC 2.4.1.22) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1) [Cleaved into: Processed beta-1,4-galactosyltransferase 1]
[Ogt] UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (EC 2.4.1.255) (O-GlcNAc transferase subunit p110) (O-linked N-acetylglucosamine transferase 110 kDa subunit) (OGT)
[B4GALT2] Beta-1,4-galactosyltransferase 2 (Beta-1,4-GalTase 2) (Beta4Gal-T2) (b4Gal-T2) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (Lactose synthase A protein) (EC 2.4.1.22) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CRD98_26150 D3I61_11545 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTL84_23375 DTM25_06080 EC95NR1_00961 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 SAMEA3753106_00003 SAMEA3753391_00513 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[GCNT3] Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3 (EC 2.4.1.102) (EC 2.4.1.148) (EC 2.4.1.150) (C2GnT-mucin type) (C2GnT-M) (hC2GnT-M) (Core 2/core 4 beta-1,6-N-acetylglucosaminyltransferase) (C2/4GnT)
[B4galt1 Ggtb Ggtb2] Beta-1,4-galactosyltransferase 1 (Beta-1,4-GalTase 1) (Beta4Gal-T1) (b4Gal-T1) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (Lactose synthase A protein) (EC 2.4.1.22) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1) [Cleaved into: Processed beta-1,4-galactosyltransferase 1]
[PNG1 At5g49570 K6M13.12] Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC 3.5.1.52) (Peptide:N-glycanase) (AtPNG1)
[B4galt2] Beta-1,4-galactosyltransferase 2 (Beta-1,4-GalTase 2) (Beta4Gal-T2) (b4Gal-T2) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (Lactose synthase A protein) (EC 2.4.1.22) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2)
[B3GNT4 UNQ1898/PRO4344] N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 4 (EC 2.4.1.149) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 4) (BGnT-4) (Beta-1,3-Gn-T4) (Beta-1,3-N-acetylglucosaminyltransferase 4) (Beta3Gn-T4)
[B3GNT5] Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase (EC 2.4.1.206) (Lactotriaosylceramide synthase) (Lc(3)Cer synthase) (Lc3 synthase) (UDP-GlcNAc:beta-Gal beta-1,3-N-acetylglucosaminyltransferase 5) (BGnT-5) (Beta-1,3-Gn-T5) (Beta-1,3-N-acetylglucosaminyltransferase 5) (Beta3Gn-T5)

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[28890400] Deglycosylating enzymes acting on N-glycans in fungi: Insights from a genome survey.
[25832992] Mass Production of an Active Peptide-N-Glycosidase F Using Silkworm-Baculovirus Expression System.
[25497214] Cytoplasmic peptide:N-glycanase cleaves N-glycans on a carboxypeptidase Y mutant during ERAD in Saccharomyces cerevisiae.
[23462048] Abnormal N-linked glycosylation of cortical AMPA receptor subunits in schizophrenia.
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[21907640] Rapid and sensitive analyses of glycoprotein-derived oligosaccharides by liquid chromatography and laser-induced fluorometric detection capillary electrophoresis.
[19819901] Molecular identification and characterization of an acidic peptide:N-glycanase from tomato (Lycopersicum esculentum) fruits.
[18293928] 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.
[18279662] Molecular identification and characterization of peptide: N-glycanase from Schizosaccharomyces pombe.