Information on EC 2.4.99.18 - dolichyl-diphosphooligosaccharide-protein glycotransferase

for references in articles please use BRENDA:EC2.4.99.18
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EC Tree
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.
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UNIPROT: E1B265
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
AglB, AglB-L, AlgB, asparagine N-glycosyltransferase, DGL1, dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2, dolichyl-diphosphooligosaccharide-protein glycosyltransferase, dolichyldiphosphooligosaccharide-protein oligosaccharyltransferase, glycosyltransferase, dolichyldiphosphooligosaccharide-protein, glycosyltransferase, dolichylpyrophosphodiacetylchitobiose-protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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OST
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
75302-32-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
E1B265_9HELI
667
0
76742
TrEMBL
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Helicobacter species contain two unrelated pglB genes (pglB1 and pglB2), neither of which is located within a larger locus involved in protein glycosylation. In complementation experiments, the Helicobacter pullorum PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jervis, A.J.; Langdon. R.; Hitchen, P.; Lawson, A.J.; Wood, A.; Fothergill, J.L.; Morris, H.R.; Dell, A.; Wren, B.; Linton, D.
Characterization of N-linked protein glycosylation in Helicobacter pullorum
J. Bacteriol.
192
5228-5236
2010
Helicobacter pullorum (E1B265), Helicobacter pullorum
Manually annotated by BRENDA team
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