2.4.99.19: undecaprenyl-diphosphooligosaccharide-protein glycotransferase
This is an abbreviated version!
For detailed information about undecaprenyl-diphosphooligosaccharide-protein glycotransferase, go to the full flat file.
Word Map on EC 2.4.99.19
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2.4.99.19
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campylobacter
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n-glycosylation
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jejuni
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n-linked
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glycans
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lipid-linked
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lari
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sequons
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asparagine-linked
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meningitidis
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single-subunit
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glycoengineering
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ribophorin
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dolichols
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pilins
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medicine
- 2.4.99.19
- campylobacter
-
n-glycosylation
- jejuni
-
n-linked
- glycans
-
lipid-linked
- lari
-
sequons
-
asparagine-linked
- meningitidis
-
single-subunit
-
glycoengineering
-
ribophorin
- dolichols
- pilins
- medicine
Reaction
Synonyms
bacterial oligosaccharyltransferase, bacterial OST, N-oligosaccharyltransferase, N-OTase, oligosaccharyl transferase, oligosaccharyltransferase, oligosacharyltransferase, OST, OT, OTase, PglB, PglB oligosaccharyltransferase, PglB protein, PglB1, PglB2
ECTree
2.4.99.19 undecaprenyl-diphosphooligosaccharide-protein glycotransferaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.4.99.19 - undecaprenyl-diphosphooligosaccharide-protein glycotransferase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(bacillosamine1) undecaprenyl diphosphate + Ac-D-F-N-V-TNH(CH2CH2O)2CH2CH2NH-BODIPY
?
-
-
-
-
?
(GalNAc2-bacillosamine1) undecaprenyl diphosphate + Ac-D-F-N-V-TNH(CH2CH2O)2CH2CH2NH-BODIPY
?
-
-
-
-
?
(Glc1GalNAc5-bacillosamine1) undecaprenyl diphosphate + Ac-D-F-N-V-TNH(CH2CH2O)2CH2CH2NH-BODIPY
?
-
-
-
-
?
Lys-Asp-Phe-Asn-Val-Ser-Lys-Ala + N-acetyl-alpha-D-galactosaminyl-diphospho-tritrans,heptacis-undecaprenol
tritrans,heptacis-undecaprenyl diphosphate + Lys-Asp-Phe-N4-[N-acetyl-beta-D-galactosaminyl]-Asn-Val-Ser-Lys-Ala
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a chemically synthesized sugar donor with synthesized peptide acceptor
-
-
?
N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol + KDFNVSKA
tritrans,heptacis-undecaprenyl diphosphate + Lys-Asp-Phe-N4-[N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-beta-D-bacillosaminyl]-Asn-Val-Ser-Lys-Ala
-
oligosaccharyl transferase activity of PglB in vitro with synthetic disaccharide glycan donor and peptide acceptor substrate
-
-
?
tritrans,heptacis-undecaprenyl diphospho-O1 antigen + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O1 antigen
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from Shigella dysenteriae
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphospho-O11 antigen + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O11 antigen
-
from Pseudomonas aeruginosa
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphospho-O157 antigen + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O157 antigen
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from Escherichia coli
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphospho-O16 antigen + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O16 antigen
-
from Escherichia coli
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphospho-O7 antigen + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O7 antigen
-
from Escherichia coli
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphospho-O9 antigen + [Acra]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [Acra]-L-asparagine-O9 antigen
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PglB transfers the O9a antigen, an ABC transporter-dependent O antigen, to AcrA in Escherichia coli strain CWG28, the K30 antigen is not transferred to AcrA
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [HmcA]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [HmcA]-L-asparagine-oligosaccharide
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a protein from Desulfovibrio gigas, N-glycosylation site is N261
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
-
-
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
a conserved DGGK motif is essential for the function of the PglB oligosaccharyltransferase
-
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
the native substrate for PglB is a heptasaccharide
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
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as glycoprotein targets are used Escherichia coli maltose binding protein which is a native periplasmic protein and the anti-beta-galactosidase single-chain antibody fragment called scFv13-R4 that is modified with an N-terminal cotranslational export signal from Escherichia coli DsbA. The proteins are each modified C-terminally with four tandem repeats of the bacterial glycan acceptor motif DQNAT and recombinantly expressed, overview
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
e.g. Campylobacter jejuni glycoprotein (Cj0114) contaiing four potential N-glycosylation sites
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
i.e. substrate peptide LLO, modelling of active site binding, overview, and glycosylation acceptor protein 3D5, a single-chain Fv fragment containing aDQNATacceptor sequon
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
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transfer of an oligosaccharide from a polyisoprenyl pyrophosphate carrier to the asparagine side chain of proteins within the conserved glycosylation sites D/E-X1-N-X2-S/T, where X1 and X2 can be any amino acids except proline, sequence DQNAT is the optimal acceptor substrate
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
e.g. Campylobacter jejuni glycoprotein (Cj0114) contaiing four potential N-glycosylation sites
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
as glycoprotein targets are used Escherichia coli maltose binding protein which is a native periplasmic protein and the anti-beta-galactosidase single-chain antibody fragment called scFv13-R4 that is modified with an N-terminal cotranslational export signal from Escherichia coli DsbA. The proteins are each modified C-terminally with four tandem repeats of the bacterial glycan acceptor motif DQNAT and recombinantly expressed, overview
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
i.e. substrate peptide LLO, modelling of active site binding, overview, and glycosylation acceptor protein 3D5, a single-chain Fv fragment containing a DQNAT acceptor sequon
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
PglBDd can transfer mono- and polysaccharides. LLO and AcrA and substrate glycosylation sites, overview. PglBDd does not require a negatively charged residue in the -2 position of the glycosylation sequon N-X-S/T
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
e.g. Campylobacter jejuni glycoprotein (Cj0114) contaiing four potential N-glycosylation sites
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
-
e.g. Campylobacter jejuni glycoprotein (Cj0114) contaiing four potential N-glycosylation sites
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
additional information
?
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-
PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli
-
-
?
additional information
?
-
-
PglBCj can glycosylate residues in both unstructured and structured regions of eukaryotic acceptor proteins in vivo
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-
?
additional information
?
-
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ability of PglB to transfer a wide variety of saccharides and peptides, substrate specificity, mass spectrometric glycopeptide product analysis, overview. PglB readily accepts a disaccharide in vitro. PglB does require determinants in the peptide sequence beyond the canonical N-X-S/Ttripeptide
-
-
?
additional information
?
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peptide substrate library construction, based on the known glycosylation site 88DFNVS92 from the Campylobacter jejuni glycoprotein PEB3, and assessment of the amino acids at each position of the consensus glycosylation sequence for their impact on glycosylation efficiency using a quantitative radioactivity-based in vitro assay, and glycosylation sequences specificity, overview. Circular dichroism spectra of acceptor proteins. PglB is inactive with glycosyl donors such as dolichyl-pyrophosphatechitobiose
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-
?
additional information
?
-
-
PglB is solely responsible for the oligosaccharyltransferase activity, PglB exhibits relaxed sugar substrate specificity
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-
?
additional information
?
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PglB-dependent N-glycosylation, structural analysis of in vitro-generated glycopeptides, overview
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-
?
additional information
?
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PglBCj adds two glycan chains to model protein acceptor AcrA. PglBCj recognizes the conventional bacterial glycosylation sequon consisting of the sequence D/E-X1-NNX2-S/T, where X1 and X2 are any amino acid except proline, in contrast to PglBDd from Desulfovibrio desulfuricans, overview. AcrA contains five potential N-glycosylation sites N-X-S/T, but only the two that have an Asp residue at the -2 position are recognized by the Campylobacter jejuni enzyme, N123 and N273
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-
?
additional information
?
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PglBCj is able to transfer Man3GlcNAc2 to extended sites but not to minimal glycosylation sites in engineered or eukaryotic target proteins
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-
?
additional information
?
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the PglB relaxed oligosaccharide substrate specificity allows the transfer of different glycans from the lipid carrier undecaprenyl pyrophosphate to an acceptor protein, substrate specificity of PglB with a set of lipid-linked polysaccharides in Escherichia coli and Salmonella enterica serovar Typhimurium. PglB required an acetamido group at the C-2, while a hexose linked to the C-6 of the monosaccharide at the reducing end does not inhibit the transfer of the O antigen to the acceptor protein, mechanism of PglB, modeling, overview. The Salmonella enterica O antigen containing Gal at the reducing end , and K30 capsular antigen, and LT2 antigen are not substrates for PglB, as
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-
?
additional information
?
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PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli
-
-
?
additional information
?
-
-
PglB-dependent N-glycosylation, structural analysis of in vitro-generated glycopeptides, overview
-
-
?
additional information
?
-
-
PglBCl is able to transfer Man3GlcNAc2 to extended sites but not to minimal glycosylation sites in engineered or eukaryotic target proteins
-
-
?
additional information
?
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the recombinantly expressed PglB can transfer the Campylobacter jejuni heptasaccharide onto the model protein acceptor AcrA, PglBDd adds a single glycan chain to AcrA. PglBDd does not recognize the conventional bacterial glycosylation sequon consisting of the sequence D/E-X1-NNX2-S/T, where X1 and X2 are any amino acid except proline, and instead uses a different site for the attachment of the oligosaccharide than PglBCj from Campylobacter jejuni, PglBDd exhibits relaxed glycan specificity, being able to transfer mono- and polysaccharides to AcrA, overview
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-
?
additional information
?
-
-
PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli
-
-
?
additional information
?
-
-
PglB1-dependent N glycosylation with a linear pentasaccharide requiring an acidic residue at the -2 position of the N-glycosylation sequon, structural analysis of in vitro-generated glycopeptides, overview
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-
?
additional information
?
-
-
PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli
-
-
?
additional information
?
-
-
PglB1-dependent N glycosylation with a linear pentasaccharide requiring an acidic residue at the -2 position of the N-glycosylation sequon, structural analysis of in vitro-generated glycopeptides, overview
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?
