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Campylobacter jejuni heptasaccharide bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
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alpha-1,3-linked sugar, in vivo in Escherichia coli
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-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-L-asparagine-N-oligosaccharide
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
Escherichia coli group 1 K30 capsule antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
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in vivo in Escherichia coli
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-
?
Escherichia coli O16 antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
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alpha-1,6-linked Glc with GlcNAc, in vivo in Escherichia coli
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-
?
Escherichia coli O2 antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
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rhamnose beta-1,4-linked sugar, in vivo in Escherichia coli
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-
?
Escherichia coli O7 antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
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beta-1,3-linked sugar, in vivo in Escherichia coli
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-
?
Escherichia coli O86 antigen bound to farnesyl diphosphate + pilin
farnesyl diphosphate + glycosylated pilin
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pentasaccharide attached to other lipid carrier, in vitro, 500 mM Tris-HCl containing 1 M sucrose and 10 mM MnCl2, pH7.5, 30°C
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-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
N-acetyl-D-glucosamine + glycoprotein bound to polysaccharide cell wall
?
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glycoproteins as substrates are P15703, O13547, P53301, P32623, P28319, P38248, P22146, Q03655, Q08193, P38616
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?
peptidoglycan bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
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transfer of subunit of the peptidoglycan petapeptide, no transfer of the complete peptidoglycan is observed, in vivo in Salmonella enterica
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?
Pseudomonas aeruginosa O11 antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
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FucNac, in vivo in Escherichia coli
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-
?
Salmonella enterica O antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
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in vivo in Escherichia coli
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-
?
Salmonella typhimurium LT2 antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
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in vivo in Escherichia coli, in vivo in Salmonella enterica serovar Typhimurium LT2 strain
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-
?
additional information
?
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dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
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-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
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-
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
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-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
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-
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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-
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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-
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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-
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-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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-
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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-
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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-
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-L-asparagine-N-oligosaccharide
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a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-L-asparagine-N-oligosaccharide
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a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-L-asparagine-N-oligosaccharide
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transfer of a preassembled, uniform oligosaccharide (Glc3Man9GlcNAc2 in most eukaryotes) from the isoprenoid lipid carrier dolichol diphosphate to the side-chain amide group nitrogen of an asparagine residue contained in a N-X-S(T) sequon of the polypeptide substrate, where X can be any amino acid except proline, mechanism, overview
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-L-asparagine-N-oligosaccharide
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a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-L-asparagine-N-oligosaccharide
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transfer of a preassembled, uniform oligosaccharide (Glc3Man9GlcNAc2 in most eukaryotes) from the isoprenoid lipid carrier dolichol pyrophosphate to the side-chain amide group nitrogen of an asparagine residue contained in a N-X-S(T) sequon of the polypeptide substrate, where X can be any amino acid except proline, mechanism, modeling, overview
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-L-asparagine-N-oligosaccharide
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a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-L-asparagine-N-oligosaccharide
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transfer of a preassembled, uniform oligosaccharide (Glc3Man9GlcNAc2 in most eukaryotes) from the isoprenoid lipid carrier dolichol diphosphate to the side-chain amide group nitrogen of an asparagine residue contained in a N-X-S(T) sequon of the polypeptide substrate, where X can be any amino acid except proline, mechanism, overview
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
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?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
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PglB, the key enzyme of the Campylobacter jejuni N-glycosylation system, transfers O polysaccharide from a lipid carrier (undecaprenyl pyrophosphate) to an accept or protein. PglB is the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer
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?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
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?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
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?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
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?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
asparagine-linked glycosylation is a common posttranslational modification of diverse secretory and membrane proteins in eukaryotes, where it is catalyzed by the multiprotein complex oligosaccharyltransferase. Eukaryotic oligosaccharyltransferase is a multifunctional enzyme that acts at the crossroads of protein modification and protein folding
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?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
oligosaccharyl transferase (OT) is a multisubunit enzyme that catalyzes N-linked glycosylation of nascent polypeptides in the lumen of the endoplasmic reticulum
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?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
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oligosaccharyltransferase complex catalyzes the transfer of a lipid-linked core oligosaccharide onto asparagine residues of nascent polypeptide chains in the lumen of the endoplasmic reticulum
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?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
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?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
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central enzyme in the pathway of glycoprotein assembly
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?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
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central enzyme in synthesis of N-linked glycoproteins
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?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
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the DAD1 subunit is a defender against apoptotic cell death
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?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
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central enzyme in the pathway of glycoprotein assembly
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?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
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?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
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central enzyme in the pathway of glycoprotein assembly
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?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
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central enzyme in synthesis of N-linked glycoproteins
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?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
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central enzyme in the pathway of glycoprotein assembly
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?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
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central enzyme in the pathway of glycoprotein assembly
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?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
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central enzyme in the pathway of glycoprotein assembly
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?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
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central enzyme in the pathway of glycoprotein assembly
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?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
N-glycosylation of eukaryotic secretory and membrane-bound proteins is an essential and highly conserved protein modification. The key step in this pathway is the en bloc transfer of the high mannose core oligosaccharide Gly3Man9GlcNAc2 from the lipid carries dolichyl phosphate to selected Asn-X-Ser/Thr sequences of nascent polypeptide chains during their translocation across the endoplasmic reticulum membrane
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?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
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dolichyl-diphosphochitobiose-Man9Glc3 is the preferred glycosyl donor both in vivo and in vitro
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?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
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the enzyme catalyzes the glycosylation of selected asparagine residues of nascent polypeptide chains as they are translocated into the lumen of the endoplasmic reticulum
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?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
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N-glycosylation of eukaryotic secretory and membrane-bound proteins is an essential and highly conserved protein modification. The key step in this pathway is the en bloc transfer of the high mannose core oligosaccharide Gly3Man9GlcNAc2 from the lipid carries dolichyl phosphate to selected Asn-X-Ser/Thr sequences of nascent polypeptide chains during their translocation across the endoplasmic reticulum membrane
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?
additional information
?
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the STT3a subunit isoform mediates specific protein glycosylation steps that are necessary for cell cycle progression during osmotic stres adaption
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?
additional information
?
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salt stress caused growth inhibition, aberrant root-tip morphology, and callose accumulation in cgl1, is observed in an ER oligosaccharyltransferase mutant, staurosporin and temperature sensitive 3a
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?
additional information
?
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key enzyme of Campylobacter jejuni N-glycosylation system, transfers O-polysaccharides from a lipid carrier (undecaprenyl pyrophosphate) to an acceptor protein. PglB is the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer
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?
additional information
?
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PglB transfers a wide variety of saccharides
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?
additional information
?
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deletion of stt3, the only component of the oligosaccharide transferase complex detected in archaea, does not affect cell viability, it appears that N-glycosylation is not essential in Haloferax volcanii
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?
additional information
?
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fine regulation of OTase activity is essential for normal cognitive-function development
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?
additional information
?
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oligosaccharyl transferase catalyzes the first committed step in N-linked protein glycosylation, a cotranslational process that occurs in the lumen of the endoplasmic reticulum
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additional information
?
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Pkc1p cascade controls N-glycosylation by regulation of Stt3p activity
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?
additional information
?
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the enzyme catalyzes the key step of N-glycosylation of proteins in the endoplasmic reticulum by the hetero-oligomeric protein complex oligosaccharyltransferase. It transfers the lipid-linked core-oligosaccharide to selected Asn-X-Ser/Thr sequences of nascent polypeptide chains
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?
additional information
?
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it may be that the lumenal domain of Ost1p is involved in funneling the newly synthesized polypeptides into the active site on Stt3p for the glycosylation oligosaccharyl transferase reaction
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?
additional information
?
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it may be that the lumenal domain of Ost1p is involved in funneling the newly synthesized polypeptides into the active site on Stt3p for the glycosylation oligosaccharyl transferase reaction
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?
additional information
?
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it may be that the lumenal domain of Ost1p is involved in funneling the newly synthesized polypeptides into the active site on Stt3p for the glycosylation oligosaccharyl transferase reaction
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?
additional information
?
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it may be that the lumenal domain of Ost1p is involved in funneling the newly synthesized polypeptides into the active site on Stt3p for the glycosylation oligosaccharyl transferase reaction
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?
additional information
?
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it may be that the lumenal domain of Ost1p is involved in funneling the newly synthesized polypeptides into the active site on Stt3p for the glycosylation oligosaccharyl transferase reaction
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?
additional information
?
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it may be that the lumenal domain of Ost1p is involved in funneling the newly synthesized polypeptides into the active site on Stt3p for the glycosylation oligosaccharyl transferase reaction
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?
additional information
?
-
it may be that the lumenal domain of Ost1p is involved in funneling the newly synthesized polypeptides into the active site on Stt3p for the glycosylation oligosaccharyl transferase reaction
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?
additional information
?
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it may be that the lumenal domain of Ost1p is involved in funneling the newly synthesized polypeptides into the active site on Stt3p for the glycosylation oligosaccharyl transferase reaction
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?
additional information
?
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tight association of DAD1 with the active OST complex with specific interactions between the N-terminal domain of DAD1 and subunit OST48
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?