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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: P41543
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Word Map
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, 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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NATURAL SUBSTRATE
NATURAL 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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. The functional domain of Ost1p is its membrane-anchored lumenal domain
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
OST1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
476
0
54072
Swiss-Prot
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, G.; Yan, Q.; Nita-Lazar, A.; Haltiwanger, R.S.; Lennarz, W.J.
Studies on the N-glycosylation of the subunits of oligosaccharyl transferase in Saccharomyces cerevisiae
J. Biol. Chem.
280
1864-1871
2005
Saccharomyces cerevisiae (P33767), Saccharomyces cerevisiae (P39007), Saccharomyces cerevisiae (P41543), Saccharomyces cerevisiae (P46964), Saccharomyces cerevisiae (P48439), Saccharomyces cerevisiae (Q02795), Saccharomyces cerevisiae (Q03723), Saccharomyces cerevisiae (Q92316), Saccharomyces cerevisiae (Q99380), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Lennarz, W.J.
Studies on oligosaccharyl transferase in yeast
Acta Biochim. Pol.
54
673-677
2007
Saccharomyces cerevisiae (P33767), Saccharomyces cerevisiae (P41543), Saccharomyces cerevisiae (P46964), Saccharomyces cerevisiae (P48439), Saccharomyces cerevisiae (Q02795), Saccharomyces cerevisiae (Q92316), Saccharomyces cerevisiae (Q99380), Saccharomyces cerevisiae
Manually annotated by BRENDA team