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IUBMB Comments Occurs in eukaryotes that form a glycoprotein by the transfer of a glucosyl-mannosyl-glucosamine polysaccharide to the side-chain of an L-asparagine residue in the sequence -Asn-Xaa-Ser- or -Asn-Xaa-Thr- (Xaa not Pro) in nascent polypeptide chains. The basic oligosaccharide is the tetradecasaccharide Glc3Man9GlcNAc2 (for diagram {polysacc/Dol14}). However, smaller oligosaccharides derived from it and oligosaccharides with additional monosaccharide units attached may be involved. See ref for a review of N-glycoproteins in eukaryotes. Man3GlcNAc2 seems to be common for all of the oligosaccharides involved with the terminal N-acetylglucosamine linked to the protein L-asparagine. Occurs on the cytosolic face of the endoplasmic reticulum. The dolichol involved normally has 14-21 isoprenoid units with two trans double-bonds at the omega end, and the rest of the double-bonds in cis form.
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
oligosaccharyltransferase, oligosaccharyl transferase, oligosaccharyltransferase complex, ost3p, wbp1p, ost6p, oligosaccharide transferase, swp1p, tbstt3a, tbstt3b,
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asparagine N-glycosyltransferase
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dolichyldiphosphooligosaccharide-protein oligosaccharyltransferase
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glycosyltransferase, dolichyldiphosphooligosaccharide-protein
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glycosyltransferase, dolichylpyrophosphodiacetylchitobiose-protein
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oligomannosyltransferase
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oligosaccharide transferase
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oligosaccharyltransferase, dolichyldiphosphoryloligosaccharide-protein
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hexosyl group transfer
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dolichyl-diphosphooligosaccharide:protein-L-asparagine N-beta-D-oligopolysaccharidotransferase
Occurs in eukaryotes that form a glycoprotein by the transfer of a glucosyl-mannosyl-glucosamine polysaccharide to the side-chain of an L-asparagine residue in the sequence -Asn-Xaa-Ser- or -Asn-Xaa-Thr- (Xaa not Pro) in nascent polypeptide chains. The basic oligosaccharide is the tetradecasaccharide Glc3Man9GlcNAc2 (for diagram {polysacc/Dol14}). However, smaller oligosaccharides derived from it and oligosaccharides with additional monosaccharide units attached may be involved. See ref [2] for a review of N-glycoproteins in eukaryotes. Man3GlcNAc2 seems to be common for all of the oligosaccharides involved with the terminal N-acetylglucosamine linked to the protein L-asparagine. Occurs on the cytosolic face of the endoplasmic reticulum. The dolichol involved normally has 14-21 isoprenoid units with two trans double-bonds at the omega end, and the rest of the double-bonds in cis form.
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pentaprenyl diphospho-N-acetyl-D-galactosamine + [protein]-L-asparagine
pentaprenyl diphosphate + [protein]-N-(N-acetyl-D-galactosaminyl)-L-asparagine
PglB can utilize shorter polyisoprenol (pentaprenol) as the lipid carrier, albeit with reduced efficiency
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undecaprenyl diphospho-N-acetyl-D-galactosamine + [protein]-L-asparagine
undecaprenyl diphosphate + [protein]-N-(N-acetyl-D-galactosaminyl)-L-asparagine
PglB is solely responsible for the oligosaccharyltransferase activity. PglB can transfer a monosaccharide, e.g. GalNAc to a peptide acceptor. PglB exhibits relaxed sugar substrate specificity
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Adenocarcinoma
Role of the Sec14-like domain of Dbl family exchange factors in the regulation of Rho family GTPases in different subcellular sites.
Congenital Disorders of Glycosylation
Mutations in STT3A and STT3B cause two congenital disorders of glycosylation.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
An Update on XMEN Disease.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Mutations in STT3A and STT3B cause two congenital disorders of glycosylation.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Oligosaccharyltransferase complex-congenital disorders of glycosylation: A novel congenital disorder of glycosylation.
Dengue
Dengue Virus Hijacks a Noncanonical Oxidoreductase Function of a Cellular Oligosaccharyltransferase Complex.
Dengue
The major oligosaccharyl transferase complex genes are not involved in dengue virus replication in Aedes aegypti mosquitoes.
Epilepsies, Partial
Oligosaccharyltransferase complex-congenital disorders of glycosylation: A novel congenital disorder of glycosylation.
Glioma
Oligosaccharyltransferase inhibition Reduces Receptor Tyrosine Kinase Activation and Enhances Glioma Radiosensitivity.
Heart Defects, Congenital
Oligosaccharyltransferase complex-congenital disorders of glycosylation: A novel congenital disorder of glycosylation.
Infections
Dengue Virus Hijacks a Noncanonical Oxidoreductase Function of a Cellular Oligosaccharyltransferase Complex.
Leukemia
Identification of differentially expressed genes following treatment of monkey kidney cells with the mycotoxin fumonisin B(1).
Lung Neoplasms
Oligosaccharyltransferase Inhibition Overcomes Therapeutic Resistance to EGFR Tyrosine Kinase Inhibitors.
Malaria
An updated view of the oligosaccharyltransferase complex in Plasmodium.
Microcephaly
Oligosaccharyltransferase complex-congenital disorders of glycosylation: A novel congenital disorder of glycosylation.
Neoplasms
Identification of differentially expressed genes following treatment of monkey kidney cells with the mycotoxin fumonisin B(1).
Neoplasms
Oligosaccharyltransferase inhibition induces senescence in RTK-driven tumor cells.
Neoplasms
Oligosaccharyltransferase Inhibition Overcomes Therapeutic Resistance to EGFR Tyrosine Kinase Inhibitors.
Neoplasms
Oligosaccharyltransferase: A Gatekeeper of Health and Tumor Progression.
Neoplasms
TUSC3: a novel tumour suppressor gene and its functional implications.
Neuronal Ceroid-Lipofuscinoses
Dolichyl-pyrophosphoryloligosaccharide protein oligosaccharide transferase in neuronal ceroid-lipofuscinosis.
Ovarian Neoplasms
Loss of the oligosaccharyl transferase subunit TUSC3 promotes proliferation and migration of ovarian cancer cells.
Spasms, Infantile
Oligosaccharyltransferase complex-congenital disorders of glycosylation: A novel congenital disorder of glycosylation.
Trypanosomiasis, African
Single-subunit oligosaccharyltransferases of Trypanosoma brucei display different and predictable peptide acceptor specificities.
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UniProt
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PglB possesses 11 transmembrane segments and two relatively large periplasmic regions other than the C-terminal domain
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Q9S4V7_CAMJU
664
0
76033
TrEMBL
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PglB is overexpressed in Escherichia coli C43(DE3) at a level of 1 mg/L cell cultures
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Li, L.; Woodward, R.; Ding, Y.; Liu, X.W.; Yi, W.; Bhatt, V.S.; Chen, M.; Zhang, L.W.; Wang, P.G.
Overexpression and topology of bacterial oligosaccharyltransferase PglB
Biochem. Biophys. Res. Commun.
394
1069-1074
2010
Campylobacter jejuni (Q9S4V7), Campylobacter jejuni
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