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Information on EC 2.4.99.19 - undecaprenyl-diphosphooligosaccharide-protein glycotransferase and Organism(s) Campylobacter lari and UniProt Accession B9KDD4
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2.4.99.19 undecaprenyl-diphosphooligosaccharide-protein glycotransferaseIUBMB Comments
A bacterial enzyme that has been isolated from Campylobacter jejuni and Campylobacter lari . It forms a glycoprotein by the transfer of a glucosyl-N-acetylgalactosaminyl-N,N'-diacetylbacillosamine (GalNAc2(Glc)GalNAc3diNAcBac) polysaccharide and related oligosaccharides to the side-chain of an L-asparagine residue in the sequence -Asp/Glu-Xaa-Asn-Xaa'-Ser/Thr- (Xaa and Xaa' not Pro) in nascent polypeptide chains. Requires Mn2+ or Mg2+. Occurs on the external face of the plasma membrane. The polyprenol involved is normally tritrans,heptacis-undecaprenol but a decaprenol is used by some species.
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Word Map
- 2.4.99.19
- campylobacter
-
n-glycosylation
- jejuni
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n-linked
- glycans
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lipid-linked
- lari
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sequons
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asparagine-linked
- meningitidis
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single-subunit
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glycoengineering
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ribophorin
- dolichols
- pilins
- medicine
The taxonomic range for the selected organisms is: Campylobacter lari
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
pglb2, n-oligosaccharyltransferase, bacterial oligosaccharyltransferase, bacterial ost, pglb protein, oligosacharyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PglB
PglB
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
tritrans,heptacis-undecaprenyl-diphosphooligosaccharide:protein-L-asparagine N-beta-D-oligosaccharidotransferase
A bacterial enzyme that has been isolated from Campylobacter jejuni [1] and Campylobacter lari [2]. It forms a glycoprotein by the transfer of a glucosyl-N-acetylgalactosaminyl-N,N'-diacetylbacillosamine (GalNAc2(Glc)GalNAc3diNAcBac) polysaccharide and related oligosaccharides to the side-chain of an L-asparagine residue in the sequence -Asp/Glu-Xaa-Asn-Xaa'-Ser/Thr- (Xaa and Xaa' not Pro) in nascent polypeptide chains. Requires Mn2+ or Mg2+. Occurs on the external face of the plasma membrane. The polyprenol involved is normally tritrans,heptacis-undecaprenol but a decaprenol is used by some species.
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
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 + [protein]-L-asparagine-oligosaccharide
additional information
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PglBCl is able to transfer Man3GlcNAc2 to extended sites but not to minimal glycosylation sites in engineered or eukaryotic target proteins
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tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
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a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
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?
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
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?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
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-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
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?
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
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?
NATURAL SUBSTRATE
NATURAL 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
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
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
the physiological cation is Mn2+, but PglB is also active with Mg2+
Mn2+
the physiological cation is Mn2+, but PglB is also active with Mg2+
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
asparagine-linked glycosylation (N-linked glycosylation) is an essential and highly conserved post-translational protein modification. This modification is essential for specific molecular recognition, protein folding, sorting in the endoplasmic reticulum, cell-cell communication, and stability
additional information
additional information
the catalytic pocket is located in the right-side cavity of PglB, structure, overview. Glycosylation sequon recognition and amide nitrogen activation are prerequisites for the formation of the N-glycosidic linkage, identification of catalytically important, acidic amino acid residues, aspartates D154 and D156 belonging to a DXD motif, and metal ion interacting D56 and E319, mechanism of N-linked glycosylation, overview. A hallmark of N-linked glycosylation is the requirement of a serine or threonine at the 12 position of the acceptor sequon, enzyme structure-function relationship
additional information
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the catalytic pocket is located in the right-side cavity of PglB, structure, overview. Glycosylation sequon recognition and amide nitrogen activation are prerequisites for the formation of the N-glycosidic linkage, identification of catalytically important, acidic amino acid residues, aspartates D154 and D156 belonging to a DXD motif, and metal ion interacting D56 and E319, mechanism of N-linked glycosylation, overview. A hallmark of N-linked glycosylation is the requirement of a serine or threonine at the 12 position of the acceptor sequon, enzyme structure-function relationship
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
PglB possesses a transmembrane domain comprising residues 1-432 and a periplasmic domain comprising residues 433-712, two domains have extensive non-covalent interactions, provided mainly by the first external loop of the transmembrane domain that forms two helices parallel to the membrane plane. The central, catalytic enzyme of OST is the STT3 subunit, structure, overview
additional information
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PglB possesses a transmembrane domain comprising residues 1-432 and a periplasmic domain comprising residues 433-712, two domains have extensive non-covalent interactions, provided mainly by the first external loop of the transmembrane domain that forms two helices parallel to the membrane plane. The central, catalytic enzyme of OST is the STT3 subunit, structure, overview
additional information
the prokaryotic oligosaccharyltransferase enzyme consists of a single polypeptide chain
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
functional PglB is partially autoglycosylated at N535 and N556
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PglB in complex with acceptor hexapeptide DQNATF, X-ray diffraction structure determination and analysis at 3.4 A resolution, molecular replacement using the periplasmic domain of Campylobacter jejuni PglB, PDB ID 3AAG, as model
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D154A
the mutation reduces the observed glycosylation yield by over 50% compared to the wild-type enzyme
D56A
the mutation reduces the observed glycosylation yield by over 90% compared to the wild-type enzyme
E319A
the mutation reduces the observed glycosylation yield by over 90% compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His10-tagged wild-type and mutant enzymes from Escherichia coli strain SCM6
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pglB, expression of His10-tagged wild-type and mutant enzymes in Escherichia coli strain SCM6
gene pglB, expressio of the enzyme and the modified substrates in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Valderrama-Rincon, J.D.; Fisher, A.C.; Merritt, J.H.; Fan, Y.Y.; Reading, C.A.; Chhiba, K.; Heiss, C.; Azadi, P.; Aebi, M.; DeLisa, M.P.
An engineered eukaryotic protein glycosylation pathway in Escherichia coli
Nat. Chem. Biol.
8
434-436
2012
Campylobacter jejuni, Campylobacter lari
Lizak, C.; Gerber, S.; Numao, S.; Aebi, M.; Locher, K.
X-ray structure of a bacterial oligosaccharyltransferase
Nature
474
350-356
2011
Campylobacter jejuni, Campylobacter lari (B9KDD4), Campylobacter lari
EXTERNAL LINKS (specific for EC-Number 2.4.99.19)
Transporter Classification Database (TCDB): 9.B.142.3.11, 9.B.142.3.9
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Release 2023.1 (January 2023)
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