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Information on EC 2.4.99.18 - dolichyl-diphosphooligosaccharide-protein glycotransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P39007
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2.4.99.18 dolichyl-diphosphooligosaccharide-protein glycotransferaseIUBMB 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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Word Map
- 2.4.99.18
-
n-glycosylation
-
n-linked
- glycans
-
lipid-linked
-
sequons
-
asparagine-linked
- jejuni
- campylobacter
- dolichol
-
ribophorins
- otase
-
cotranslational
-
bloc
-
dolichol-linked
-
translocon
- glc3man9glcnac2
- heptasaccharide
-
s-layer
-
underglycosylation
-
preassembled
-
mannosyltransferases
-
glycoengineering
-
hypoglycosylation
-
hetero-oligomeric
-
single-subunit
-
translocon-associated
- man9glcnac2
- lari
- drug development
- biotechnology
- medicine
- n-glycoproteins
-
glycoproteomics
- pilins
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
Synonyms
oligosaccharyltransferase, oligosaccharyl transferase, oligosaccharyltransferase complex, ost3p, wbp1p, ost6p, oligosaccharide transferase, swp1p, tbstt3a, tbstt3b, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
asparagine N-glycosyltransferase
-
-
-
-
dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2
-
dolichyldiphosphooligosaccharide-protein oligosaccharyltransferase
-
-
-
-
glycosyltransferase, dolichyldiphosphooligosaccharide-protein
-
-
-
-
glycosyltransferase, dolichylpyrophosphodiacetylchitobiose-protein
-
-
-
-
oligomannosyltransferase
-
-
-
-
oligosaccharide transferase
-
-
-
-
oligosaccharyl transferase
oligosaccharyltransferase
oligosaccharyltransferase complex
-
oligosaccharyltransferase, dolichyldiphosphoryloligosaccharide-protein
-
-
-
-
OST
OTase
OST
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
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
75302-32-8
-
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
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
-
-
?
dolichyl diphosphate-di-N-acetylchitobiose + Tyr-Asn-Leu-Thr-Ser-Val
?
-
-
-
-
?
dolichyl diphosphooligosaccharide + asparagine-asparagine-threonine-NH2 acceptor peptide
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
-
-
-
?
dolichyl diphosphooligosaccharide + N2-acetyl-L-asparaginyl-4-benzoyl-L-phenylalanyl-L-tyrosinamide
dolichyl diphosphate + ?
-
-
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + oligosaccaharidyl-L-Asn protein
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl disphosphate + protein with oligosaccharide attached to 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
dolichyl-diphosphochitobiose-Man1 + Tyr-Asn-Leu-Thr-Ser-Val
?
-
-
-
-
?
dolichyl-diphosphochitobiose-Man9 + Nalpha-Ac-Asn-Tyr-Thr-NH2
?
-
-
-
-
?
dolichyl-diphosphochitobiose-Man9Glc3 + alpha-Ac-Asn-Tyr-Thr-NH2
?
-
-
-
-
?
dolichyl-diphosphochitobiose-Man9Glc3 + protein-L-asparagine
?
-
-
-
-
?
dolichyl-diphosphochitobiose-Man9Glc3 + Tyr-Asn-Leu-Thr-Ser-Val
?
-
-
-
-
?
N-acetyl-D-glucosamine + glycoprotein bound to polysaccharide cell wall
?
-
glycoproteins as substrates are P15703, O13547, P53301, P32623, P28319, P38248, P22146, Q03655, Q08193, P38616
-
-
?
dolichyl diphosphochitobiose-(mannosyl)9-(glucosyl)3 + synthetic hexapeptide
?
-
-
-
-
?
dolichyl diphosphochitobiose-(mannosyl)9-(glucosyl)3 + synthetic hexapeptide
?
-
glycosyl-donors are also dolichyl diphosphochitobiose or dolichyl diphospho-chitobiose-mannose, no substrates are dolichyl diphosphochitobiose-(mannosyl)9 or dolichyl diphospho-N-acetyl-D-glucosamine
-
-
?
dolichyl diphosphochitobiose-(mannosyl)9-(glucosyl)3 + synthetic hexapeptide
?
-
e.g. Tyr-Asn-Leu-Thr-Ser-Val
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
-
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
-
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
-
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
-
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
-
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
-
glycosyl donor specificity
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
dolichyl-diphosphochitobiose-Man9Glc3 is the preferred glycosyl donor both in vivo and in vitro. The minimal glycosyl donor is dolichyl-diphosphochitobiose
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
-
peptide acceptor specificity
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
-
catalyzes reaction between beta-amido nitrogen of Asn-residue and oligosaccharyl-diphosphodolichol
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + oligosaccaharidyl-L-Asn protein
-
N-glycosylation of AcrA occurs at positions N123, N147, and N274. N-glycosylation of AcrA by the eukaryotic OST in Saccharomyces cerevisiae occurs independent of the acidic residue at the -2 position
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + oligosaccaharidyl-L-Asn protein
-
preference for dolichol-diphospho-Glc3Man9GlcNAc2 is a feature that is determined by the complex and not by the catalytic subunit
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + oligosaccaharidyl-L-Asn protein
-
the enzyme utilizes the in vivo oligosaccharide donor Glc3Man9GlcNAc2-PP-Dol in preference to certain larger and/or smaller oligosaccharide donors
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-L-asparagine-N-oligosaccharide
-
-
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
-
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
-
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
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
-
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
-
-
?
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
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
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
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in the pathway of glycoprotein assembly
-
-
?
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
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
dolichyl-diphosphochitobiose-Man9Glc3 is the preferred glycosyl donor both in vivo and in vitro
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
the enzyme catalyzes the glycosylation of selected asparagine residues of nascent polypeptide chains as they are translocated into the lumen of the endoplasmic reticulum
-
-
?
additional information
?
-
-
allosteric communication between regulatory and catalytic dolichol-linked oligosaccharide binding sites
-
-
?
additional information
?
-
-
evidence against either enol lactone or ketone formation as an intermediate
-
-
?
additional information
?
-
-
oligosaccharyl transferase catalyzes the first committed step in N-linked protein glycosylation, a cotranslational process that occurs in the lumen of the endoplasmic reticulum
-
-
?
additional information
?
-
-
Pkc1p cascade controls N-glycosylation by regulation of Stt3p activity
-
-
?
additional information
?
-
-
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
tight association of DAD1 with the active OST complex with specific interactions between the N-terminal domain of DAD1 and subunit OST48
-
-
?
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
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
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl disphosphate + protein with oligosaccharide attached to 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
N-acetyl-D-glucosamine + glycoprotein bound to polysaccharide cell wall
?
-
glycoproteins as substrates are P15703, O13547, P53301, P32623, P28319, P38248, P22146, Q03655, Q08193, P38616
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-L-asparagine-N-oligosaccharide
-
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
-
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
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
-
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
-
-
?
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
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
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
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in the pathway of glycoprotein assembly
-
-
?
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
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
dolichyl-diphosphochitobiose-Man9Glc3 is the preferred glycosyl donor both in vivo and in vitro
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
the enzyme catalyzes the glycosylation of selected asparagine residues of nascent polypeptide chains as they are translocated into the lumen of the endoplasmic reticulum
-
-
?
additional information
?
-
-
oligosaccharyl transferase catalyzes the first committed step in N-linked protein glycosylation, a cotranslational process that occurs in the lumen of the endoplasmic reticulum
-
-
?
additional information
?
-
-
Pkc1p cascade controls N-glycosylation by regulation of Stt3p activity
-
-
?
additional information
?
-
-
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
tight association of DAD1 with the active OST complex with specific interactions between the N-terminal domain of DAD1 and subunit OST48
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mg2+
absolute requirement for divalent cations that can adopt an octahedral coordination geometry with preference for Mn2+ over Mg2+
Mg2+
-
divalent cation required. Mg2+, at concentration of 10 mM yields only one third the activity observed with Mn2+
Mn2+
absolute requirement for divalent cations that can adopt an octahedral coordination geometry with preference for Mn2+ over Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-threoninamide, (2S)-2-(benzoylamino)-4-[(phenylmethyl)amino]butanoylglycyl-L-threonyl-L-valyl
-
-
L-threoninamide, (2S)-2-(benzoylamino)-4-[[(4-methoxyphenyl)methyl]amino]butanoylglycyl-L-threonyl-L-valyl
-
-
L-threoninamide, (2S)-2-(benzoylamino)-4-[[(4-nitrophenyl)methyl]amino]butanoylglycyl-L-threonyl-L-valyl
-
-
L-Threoninamide, (2S)-2-[(6-mercapto-1-oxohexyl)amino]-4-[(2-naphthalenylmethyl)amino]butanoyl-L-cysteinyl-L-threonyl-L-valyl-, cyclic (1-2)-thioether
-
-
L-Threoninamide, (2S)-2-[(6-mercapto-1-oxohexyl)amino]-4-[(2-naphthalenylmethyl)amino]butanoyl-L-cysteinyl-L-threonyl-L-valyl-N-(2-phenylethyl)-, cyclic (1-2)-thioether
-
-
L-Threoninamide, (2S)-2-[(6-mercapto-1-oxohexyl)amino]-4-[(2-naphthalenylmethyl)amino]butanoyl-L-cysteinyl-L-threonyl-L-valyl-N-[2-(4-nitrophenyl)ethyl]-, cyclic (1-2)-thioether
-
-
L-Threoninamide, (2S)-4-(decylamino)-2-[(6-mercapto-1-oxohexyl)amino]butanoyl-L-cysteinyl-L-threonyl-L-valyl-, cyclic (1-2)-thioether
-
-
L-threoninamide, (2S)-4-amino-2-[(6-mercapto-1-oxohexyl)amino]butanoyl-L-cysteinyl-L-threonyl-L-valyl-, cyclic (1-2)-thioether
-
-
L-Threoninamide, (2S)-4-amino-2-[(6-mercapto-1-oxohexyl)amino]butanoyl-L-cysteinyl-L-threonyl-L-valyl-N-(2-phenylethyl)-, cyclic (1-2)-thioether
-
-
L-Threoninamide, (2S)-4-amino-2-[(6-mercapto-1-oxohexyl)amino]butanoyl-L-cysteinyl-L-threonyl-L-valyl-N-(4-phenylbutyl)-, cyclic (1-2)-thioether
-
-
L-Threoninamide, (2S)-4-amino-2-[(6-mercapto-1-oxohexyl)amino]butanoyl-L-cysteinyl-L-threonyl-L-valyl-N-[2-(4-nitrophenyl)ethyl]-, cyclic (1-2)-thioether
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
DAD1 might provide structural and functional integrity for the OST complex
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
Tyr-Asn-Leu-Thr-Ser-Val
-
reaction with dolichyl diphosphochitobiose-Man9Glc3
0.6
Tyr-Asn-Leu-Thr-Ser-Val
-
reaction with dolichyl diphosphochitobiose
additional information
additional information
-
dissociation constant KD=9.97 mM
-
additional information
additional information
dissociation constant KD=9.97 mM
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit STT3
SwissProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
oligosaccharyltransferase forms a binary complex with ribosomes. Reconstitution of a binary complex containing oligosaccharyltransferase and ribosomes and its electron microscopic images. Oligosaccharyltransferase, the Sec61 complex, and ribosomes form a ternary complex in vitro
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integral membrane protein, tightly associated to luminal side of membrane
-
multiple oligosaccharyl transferase isoforms with different affinities for the translocon and ribosome and with heterogeneous subunit composition might exist in the endoplasmic reticulum membrane, thereby providing a means of regulating protein N-glycosylation
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oligosaccharyl transferase has a large domain in the lumenal side of endoplasmic reticulum where the catalysis occurs. The lumenal domain mainly comprises the catalytic Stt3p, the donor substrate-recognizing Wbp1p, and the acceptor substrate-recognizing Ost1p
N-linked glycosylation occurs in the endoplasmic reticulum lumen by the membrane associated oligosaccharyltransferase enzyme complex
reaction takes place in the lumen
-
membrane protein complex. Ost2p and Stt3p have only their N terminus located in the cytosol. Ost3p and Swp1p have only their C terminus oriented in the cytosol. In the case of Ost5p and Ost6p, both their N and C termini are present in the cytosol
-
multiple oligosaccharyl transferase isoforms with different affinities for the translocon and ribosome and with heterogeneous subunit composition might exist in the endoplasmic reticulum membrane, thereby providing a means of regulating protein N-glycosylation
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. Ost4p is a minimembrane protein
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. Ost5p is a membrane protein
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. Swp1p probably possesses three transmembrane segments, with its N-terminus in the lumen and C-terminus in the cytosol
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
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. The Ost2 protein possesses three transmembrane segments, with its N-terminus in the cytosol and C-terminus directed towards the lumen
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. The sequence of the lumen-oriented half of the transmembrane domain is important for the function of the Wbp1 protein
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
OST is a heterooligomeric membrane protein complex in animals, plants, and fungi. In bacteria, archaea, and protozoa, OST is a monomer
malfunction
metabolism
-
in the central reaction of the N-linked glycosylation pathway, one of the most abundant modifications of proteins in eukaryoties, oligosaccharyltransferase, a multimeric complex located at the membrane of the endoplasmic reticulum, transfers a preassembled oligosaccharide to selected asparagine residues within the consensus sequence asparagine-X-serine/threonine
physiological function
additional information
malfunction
congenital disorders of glycosylation (CDG) have severe effects in humans, complete loss is lethal for eukaryots
malfunction
-
instability of the temperature-sensitive DAD1 mutant at restrictive temperature causes a time-dependent degradation of the other OST subunits ribophorin I, ribophorin II, and OST48, disrupting the entire OST complex. Loss of OST activity caused by DAD1 instability results in severe hypoglycosylation that might induce apoptosis. Mutations affecting the biosynthesis of the activated Glc3Man9GlcNAc2 oligosaccharide substrate or the biogenesis of OSTs generally have a systemic effect in eukaryotes and alter glycosylation of many different glycoproteins
physiological function
N-linked glycosylation of nascent polypeptides in the lumen of the endoplasmic reticulum
physiological function
-
subunits Ost3p and Ost6p are necessary for efficient glycosylation of distinct defined glycosylation sites
physiological function
asparagine-linked glycosylation is a common and vital co- and post-translocational modification of diverse secretory and membrane proteins in eukaryotes that is catalyzed by the multiprotein complex oligosaccharyltransferase. Isozymes Ost3p or Ost6p possess different protein substrate specificities at the level of individual glycosylation sites, model of Ost3/6p function in which they transiently bind stretches of nascent polypeptide substrate to inhibit protein folding, thereby increasing glycosylation efficiency at nearby asparagine residues
physiological function
asparagine-linked glycosylation is a common and vital co- and post-translocational modification of diverse secretory and membrane proteins in eukaryotes that is catalyzed by the multiprotein complex oligosaccharyltransferase. Ispzymes Ost3p or Ost6p possess different protein substrate specificities at the level of individual glycosylation sites. Ost6p, which has a peptide-binding groove with a strongly hydrophobic base lined by neutral and basic residues, binds peptides enriched in hydrophobic and acidic amino acids. Model of Ost3/6p function in which they transiently bind stretches of nascent polypeptide substrate to inhibit protein folding, thereby increasing glycosylation efficiency at nearby asparagine residues
physiological function
-
the catalytic subunit of the eukaryotic OST and catalyzes the transfer of a highly defined, lipid-linked oligosaccharide (LLO) donor substrate to a multitude of peptide acceptor sequences located in different substrate proteins
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
-
Canine OST isoforms harboring the different Stt3 proteins differ in catalytic activity and substrate selectivity. OST complexes with the Stt3-B isoform are more active reaching 8 to 12fold higher Vmax values for glycopeptide formation than complexes containing Stt3-A. The increased catalytic activity for Stt3-B complexes coincides with a reduced selectivity with respect to the oligosaccharide donor substrate. OST complexes with Stt3-B accept the dolichol-pyrophosphate-activated Glc3Man9GlcNAc2 and Man9GlcNAc2 substrates with roughly the same specificity, whereas OST complexes with Stt3-A are more selective, as reflected by increased Km values forMan9GlcNAc2 relative to Glc3Man9GlcNAc2. Stt3-A and Stt3-B also differ in their acceptor substrate selectivity
additional information
Ost3p structure-function relationship, overview
additional information
Ost3p structure-function relationship, overview
additional information
-
Ost3p structure-function relationship, overview
additional information
Ost6p structure-function relationship, overview
additional information
Ost6p structure-function relationship, overview
additional information
-
Ost6p structure-function relationship, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16000
30000
31500
MALDI-TOF result in accordance with calculated results for histidine-tagged protein subunit Stt3p
32000
x * 62000-64000, Ost1p, + x * 6000, Stt3p, + x * 47000, Wbp1p, + x * 34000, Ost3p, + x * 32000, Ost6p, + x * 30000, Swp1p, + x * 16000, Ost2p, + x * 9500, Ost5p, + x * 3600, Ost4p
34000
45000
-
x * 78000, Stt3p, + x * 64000, Ost1p, + x * 45000, Wbp1p, + x * 34000, Ost3p, + x * 30000, Swp1p, + x * 16000, Ost2p, + x * 9500, Ost5p, + x * 3600, Ost4p, the enzyme is composed of equimolar amounts of eight subunits, the enzyme is composed of the following three subcomplexes: 1. Stt3p-Ost4p-Ast3p, 2. Swp1p-Wbp1p-Ost2p0, 3. Ost1p-Aso5p, SDS-PAGE
47000
x * 62000-64000, Ost1p, + x * 6000, Stt3p, + x * 47000, Wbp1p, + x * 34000, Ost3p, + x * 32000, Ost6p, + x * 30000, Swp1p, + x * 16000, Ost2p, + x * 9500, Ost5p, + x * 3600, Ost4p
480000
oligosaccharyltransferase complex, native polyacrylamide gel electrophoresis
6000
x * 62000-64000, Ost1p, + x * 6000, Stt3p, + x * 47000, Wbp1p, + x * 34000, Ost3p, + x * 32000, Ost6p, + x * 30000, Swp1p, + x * 16000, Ost2p, + x * 9500, Ost5p, + x * 3600, Ost4p
64000
-
x * 78000, Stt3p, + x * 64000, Ost1p, + x * 45000, Wbp1p, + x * 34000, Ost3p, + x * 30000, Swp1p, + x * 16000, Ost2p, + x * 9500, Ost5p, + x * 3600, Ost4p, the enzyme is composed of equimolar amounts of eight subunits, the enzyme is composed of the following three subcomplexes: 1. Stt3p-Ost4p-Ast3p, 2. Swp1p-Wbp1p-Ost2p0, 3. Ost1p-Aso5p, SDS-PAGE
78000
-
x * 78000, Stt3p, + x * 64000, Ost1p, + x * 45000, Wbp1p, + x * 34000, Ost3p, + x * 30000, Swp1p, + x * 16000, Ost2p, + x * 9500, Ost5p, + x * 3600, Ost4p, the enzyme is composed of equimolar amounts of eight subunits, the enzyme is composed of the following three subcomplexes: 1. Stt3p-Ost4p-Ast3p, 2. Swp1p-Wbp1p-Ost2p0, 3. Ost1p-Aso5p, SDS-PAGE
9500
16000
-
x * 78000, Stt3p, + x * 64000, Ost1p, + x * 45000, Wbp1p, + x * 34000, Ost3p, + x * 30000, Swp1p, + x * 16000, Ost2p, + x * 9500, Ost5p, + x * 3600, Ost4p, the enzyme is composed of equimolar amounts of eight subunits, the enzyme is composed of the following three subcomplexes: 1. Stt3p-Ost4p-Ast3p, 2. Swp1p-Wbp1p-Ost2p0, 3. Ost1p-Aso5p, SDS-PAGE
16000
x * 62000-64000, Ost1p, + x * 6000, Stt3p, + x * 47000, Wbp1p, + x * 34000, Ost3p, + x * 32000, Ost6p, + x * 30000, Swp1p, + x * 16000, Ost2p, + x * 9500, Ost5p, + x * 3600, Ost4p
30000
-
x * 78000, Stt3p, + x * 64000, Ost1p, + x * 45000, Wbp1p, + x * 34000, Ost3p, + x * 30000, Swp1p, + x * 16000, Ost2p, + x * 9500, Ost5p, + x * 3600, Ost4p, the enzyme is composed of equimolar amounts of eight subunits, the enzyme is composed of the following three subcomplexes: 1. Stt3p-Ost4p-Ast3p, 2. Swp1p-Wbp1p-Ost2p0, 3. Ost1p-Aso5p, SDS-PAGE
30000
x * 62000-64000, Ost1p, + x * 6000, Stt3p, + x * 47000, Wbp1p, + x * 34000, Ost3p, + x * 32000, Ost6p, + x * 30000, Swp1p, + x * 16000, Ost2p, + x * 9500, Ost5p, + x * 3600, Ost4p
34000
-
x * 78000, Stt3p, + x * 64000, Ost1p, + x * 45000, Wbp1p, + x * 34000, Ost3p, + x * 30000, Swp1p, + x * 16000, Ost2p, + x * 9500, Ost5p, + x * 3600, Ost4p, the enzyme is composed of equimolar amounts of eight subunits, the enzyme is composed of the following three subcomplexes: 1. Stt3p-Ost4p-Ast3p, 2. Swp1p-Wbp1p-Ost2p0, 3. Ost1p-Aso5p, SDS-PAGE
34000
x * 62000-64000, Ost1p, + x * 6000, Stt3p, + x * 47000, Wbp1p, + x * 34000, Ost3p, + x * 32000, Ost6p, + x * 30000, Swp1p, + x * 16000, Ost2p, + x * 9500, Ost5p, + x * 3600, Ost4p
9500
-
x * 78000, Stt3p, + x * 64000, Ost1p, + x * 45000, Wbp1p, + x * 34000, Ost3p, + x * 30000, Swp1p, + x * 16000, Ost2p, + x * 9500, Ost5p, + x * 3600, Ost4p, the enzyme is composed of equimolar amounts of eight subunits, the enzyme is composed of the following three subcomplexes: 1. Stt3p-Ost4p-Ast3p, 2. Swp1p-Wbp1p-Ost2p0, 3. Ost1p-Aso5p, SDS-PAGE
9500
x * 62000-64000, Ost1p, + x * 6000, Stt3p, + x * 47000, Wbp1p, + x * 34000, Ost3p, + x * 32000, Ost6p, + x * 30000, Swp1p, + x * 16000, Ost2p, + x * 9500, Ost5p, + x * 3600, Ost4p
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heptamer
-
heteromeric OST complex comprising seven subunits, Stt3 proteins are the catalytic subunits of eukaryotic OST complexes, structure-function relationships, detailed overview. Canine OST isoforms harboring the different Stt3 proteins differ in catalytic activity and substrate selectivity. OST complexes with the Stt3-B isoform are more active reaching 8 to 12fold higher Vmax values for glycopeptide formation than complexes containing Stt3-A
nonamer
the enzyme consists of nine subunits. Five of them, Wbp1, Swp1, Stt3, Ost1, and Ost2, are essential for viability of the cell, whereas Ost4, Ost5, Ost3, and Ost6 are not essential but are required for maximal OST activity: Wbp1 (49392 Da), Swp1 (31653 Da), Stt3 (81529 Da), Ost1 (54072 Da), Ost2 (14698 Da), Ost3, Ost4, Ost5, and Ost6, calculated from sequence
octamer
-
eight polypeptides assemble into a heterooctameric yeast OST complex composed of one copy each of Ost1p, Ost2p, Ost3p or Ost6p, Ost4p, Ost5p, Wbp1p, Swp1p, and Stt3p
additional information
?
-
x * 78000, Stt3p, + x * 64000, Ost1p, + x * 45000, Wbp1p, + x * 34000, Ost3p, + x * 30000, Swp1p, + x * 16000, Ost2p, + x * 9500, Ost5p, + x * 3600, Ost4p, the enzyme is composed of equimolar amounts of eight subunits, the enzyme is composed of the following three subcomplexes: 1. Stt3p-Ost4p-Ast3p, 2. Swp1p-Wbp1p-Ost2p0, 3. Ost1p-Aso5p, SDS-PAGE
?
x * 62000-64000, Ost1p, + x * 6000, Stt3p, + x * 47000, Wbp1p, + x * 34000, Ost3p, + x * 32000, Ost6p, + x * 30000, Swp1p, + x * 16000, Ost2p, + x * 9500, Ost5p, + x * 3600, Ost4p
additional information
dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit STT3: 81529 Da
additional information
-
dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit STT3: 81529 Da
additional information
-
multimeric membrane-bound enzyme complex comprising nine integral membrane subunits
additional information
-
analysis of the organization of the translocon-oligosaccharyl transferase supercomplex using chemical cross-linking and splitubiquitin analysis
additional information
-
multimeric complex containing eight different proteins, one of which (Stt3p) is the catalytic subunit
additional information
-
oligosaccharyl transferase subunits display specific interactions with each other in a functional complex. A distinct conformation rearrangement takes place when the enzyme complex changes from the nonfunctional state to the activated functional state
additional information
-
protein complex oligosaccharyltransferase consists of two isoforms with distinct functions differing only in the presence of the two related Ost3 and Ost6p proteins. The OST6-complex is found to be important for cell wall integrity and temperature stress. Ost3p and Ost6p are not essential for OST activity, and can in part displace each other in the complex when overexpressed
additional information
-
the oligosaccharyl transferase complex contains nine subunits. The purified OT complex has an apparent mass of about 500000 Da, suggesting a dimeric configuration. The dimeric structure of OT might be required for effective association with the translocon dimer and for its allosteric regulation during cotranslational glycosylation
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p
additional information
-
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Four others are not essential Ost3p, Ost4p, Ost5p, Ost6p. Ost2p may aid Wbp1p in recognition of the Dol-PP-oligosaccharide
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Four others are not essential Ost3p, Ost4p, Ost5p, Ost6p. Ost2p may aid Wbp1p in recognition of the Dol-PP-oligosaccharide
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Four others are not essential Ost3p, Ost4p, Ost5p, Ost6p. Ost2p may aid Wbp1p in recognition of the Dol-PP-oligosaccharide
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Four others are not essential Ost3p, Ost4p, Ost5p, Ost6p. Ost2p may aid Wbp1p in recognition of the Dol-PP-oligosaccharide
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Four others are not essential Ost3p, Ost4p, Ost5p, Ost6p. Ost2p may aid Wbp1p in recognition of the Dol-PP-oligosaccharide
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Four others are not essential Ost3p, Ost4p, Ost5p, Ost6p. Ost2p may aid Wbp1p in recognition of the Dol-PP-oligosaccharide
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Four others are not essential Ost3p, Ost4p, Ost5p, Ost6p. Ost2p may aid Wbp1p in recognition of the Dol-PP-oligosaccharide
additional information
-
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Four others are not essential Ost3p, Ost4p, Ost5p, Ost6p. Ost2p may aid Wbp1p in recognition of the Dol-PP-oligosaccharide
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Ost4p functions to bind Ost3p and Stt3p together in a subcomplex of oligosaccharyl transferase via interactions with its amino-acid residues near the cytosolic leaflet of the endoplasmic reticulum membrane. Ost4p is proposed to be responsible for recruiting Ost3p or Ost6p into the oligosaccharyl transferase complex
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Ost4p functions to bind Ost3p and Stt3p together in a subcomplex of oligosaccharyl transferase via interactions with its amino-acid residues near the cytosolic leaflet of the endoplasmic reticulum membrane. Ost4p is proposed to be responsible for recruiting Ost3p or Ost6p into the oligosaccharyl transferase complex
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Ost4p functions to bind Ost3p and Stt3p together in a subcomplex of oligosaccharyl transferase via interactions with its amino-acid residues near the cytosolic leaflet of the endoplasmic reticulum membrane. Ost4p is proposed to be responsible for recruiting Ost3p or Ost6p into the oligosaccharyl transferase complex
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Ost4p functions to bind Ost3p and Stt3p together in a subcomplex of oligosaccharyl transferase via interactions with its amino-acid residues near the cytosolic leaflet of the endoplasmic reticulum membrane. Ost4p is proposed to be responsible for recruiting Ost3p or Ost6p into the oligosaccharyl transferase complex
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Ost4p functions to bind Ost3p and Stt3p together in a subcomplex of oligosaccharyl transferase via interactions with its amino-acid residues near the cytosolic leaflet of the endoplasmic reticulum membrane. Ost4p is proposed to be responsible for recruiting Ost3p or Ost6p into the oligosaccharyl transferase complex
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Ost4p functions to bind Ost3p and Stt3p together in a subcomplex of oligosaccharyl transferase via interactions with its amino-acid residues near the cytosolic leaflet of the endoplasmic reticulum membrane. Ost4p is proposed to be responsible for recruiting Ost3p or Ost6p into the oligosaccharyl transferase complex
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Ost4p functions to bind Ost3p and Stt3p together in a subcomplex of oligosaccharyl transferase via interactions with its amino-acid residues near the cytosolic leaflet of the endoplasmic reticulum membrane. Ost4p is proposed to be responsible for recruiting Ost3p or Ost6p into the oligosaccharyl transferase complex
additional information
-
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Ost4p functions to bind Ost3p and Stt3p together in a subcomplex of oligosaccharyl transferase via interactions with its amino-acid residues near the cytosolic leaflet of the endoplasmic reticulum membrane. Ost4p is proposed to be responsible for recruiting Ost3p or Ost6p into the oligosaccharyl transferase complex
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Since the lumenal domain of Swp1p interacts with that of Ost1p, it may aid Ost1p in funneling nascent polypeptide chains into the active site of the oligosaccharyl transferase complex
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Since the lumenal domain of Swp1p interacts with that of Ost1p, it may aid Ost1p in funneling nascent polypeptide chains into the active site of the oligosaccharyl transferase complex
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Since the lumenal domain of Swp1p interacts with that of Ost1p, it may aid Ost1p in funneling nascent polypeptide chains into the active site of the oligosaccharyl transferase complex
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Since the lumenal domain of Swp1p interacts with that of Ost1p, it may aid Ost1p in funneling nascent polypeptide chains into the active site of the oligosaccharyl transferase complex
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Since the lumenal domain of Swp1p interacts with that of Ost1p, it may aid Ost1p in funneling nascent polypeptide chains into the active site of the oligosaccharyl transferase complex
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Since the lumenal domain of Swp1p interacts with that of Ost1p, it may aid Ost1p in funneling nascent polypeptide chains into the active site of the oligosaccharyl transferase complex
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Since the lumenal domain of Swp1p interacts with that of Ost1p, it may aid Ost1p in funneling nascent polypeptide chains into the active site of the oligosaccharyl transferase complex
additional information
-
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Since the lumenal domain of Swp1p interacts with that of Ost1p, it may aid Ost1p in funneling nascent polypeptide chains into the active site of the oligosaccharyl transferase complex
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Specific interaction between Ost3p and Sbh1p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Specific interaction between Ost3p and Sbh1p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Specific interaction between Ost3p and Sbh1p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Specific interaction between Ost3p and Sbh1p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Specific interaction between Ost3p and Sbh1p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Specific interaction between Ost3p and Sbh1p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Specific interaction between Ost3p and Sbh1p
additional information
-
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p. Specific interaction between Ost3p and Sbh1p
additional information
functional and structural investigations of the Ost3/6p components of the yeast enzyme. Genetic, biochemical and structural analyses of the lumenal domain of Ost6p reveals oxidoreductase activity mediated by a thioredoxin-like fold with a distinctive active-site loop that changed conformation with redox state
additional information
-
functional and structural investigations of the Ost3/6p components of the yeast enzyme. Genetic, biochemical and structural analyses of the lumenal domain of Ost6p reveals oxidoreductase activity mediated by a thioredoxin-like fold with a distinctive active-site loop that changed conformation with redox state
additional information
-
six different subunits are detected in the wild-type complex, including Stt3p, Ost1p, Wbp1p, Swp1p, Ost3p, and Ost6p. The small 3.4-kDa subunit Ost4p is required for the incorporation of either Ost3p or Ost6p into the complex, resulting in two, functionally distinct OTase complexes in vivo. Ost3p and Ost6p are not absolutely required for OTase activity, but modulate the affinity of the enzyme toward different protein substrates
additional information
the eukaryotic oligosaccharyltransferase is a complex of multiple non-identical subunits. The Yeast oligosaccharyltransferase enzyme complex contains a single Stt3 subunit
additional information
-
the eukaryotic oligosaccharyltransferase is a complex of multiple non-identical subunits. The Yeast oligosaccharyltransferase enzyme complex contains a single Stt3 subunit
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
oligosaccharyl transferase consists of nine different subunits. Three of the essential gene products, Ost1p, Wbp1p, and Stt3p, are N-linked glycoproteins. The four potential N-glycosylation sites in Ost1p and the two potential N-glycosylation sites in Wbp1p are occupied in the mature proteins. None of the N-glycosylation sites in these two proteins is conserved, and no defect in growth or oligosaccharyl transferase activity is observed when the N-glycosylation sites are mutated to block N-glycosylation in either subunit. Glycan chain of the Stt3p subunit (Man8GlcNAc2) is linked only to Asn539
glycoprotein
-
the large soluble domains of the subunits Nlt1p and Wbp1p are glycosylated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit OST6
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D518E
the replacement of a key residue, Asp518, located within the WWDYG signature motif (residues 516-520), leads to a distinct tertiary structure, even though both proteins have similar overall secondary structures, as demonstrated by CD, fluorescence and NMR spectroscopies. Asp518 plays a critical structural role, in addition to the catalytic role. The activity of the protein is confirmed by saturation transfer difference and nuclear magnetic resonance titration studies
D518E
within WWDYG signature motif leads to distinct tertiary structure interfering with function (complete loss of N-linked glycosylation activity), lethal
E113V
mutant (of the OST2 gene encoding the epsilon-subunit of oligosyltransferase) shows temperature sensitivity mainly due to the death of daughter cells
G58R
mutant (of the OST2 gene encoding the epsilon-subunit of oligosyltransferase) shows temperature sensitivity mainly due to the death of daughter cells
G86R
mutant (of the OST2 gene encoding the epsilon-subunit of oligosyltransferase) shows temperature sensitivity mainly due to the death of daughter cells
N217Q
mutant of subunit Ost1p, normal growth phenotype, glycosylation change detected
N332Q
mutant of subunit Wbp1p, normal growth phenotype, glycosylation change detected
N336Q
mutant of subunit Ost1p, normal growth phenotype, glycosylation change detected
N400Q
mutant of subunit Ost1p, normal growth phenotype, glycosylation change detected
N535Q
mutant of subunit Stt3p, lethal phenotype, glycosylation change detected
N536Q
mutant of subunit Stt3p, normal growth phenotype, glycosylation change detected
N539Q
mutant of subunit Stt3p, lethal phenotype, glycosylation change detected
N540Q
mutant of subunit Stt3p, normal growth phenotype, glycosylation change detected
N60Q
N99Q
mutant of subunit Ost1p, normal growth phenotype, glycosylation change detected
N99Q/N217Q
mutant of subunit Ost1p, normal growth phenotype, glycosylation change detected
Q103K/Q106K
introducing basic residues in place of the wild-type neutral residues lining the peptide-binding groove of Ost3p, allows binding of a hydrophobic and acidic peptide. MBP-Ost3Q103K,Q106K variant shows significant binding to the peptide
T537A
mutant of subunit Stt3p, lethal phenotype, glycosylation change detected
T537A/N539Q
mutant of subunit Stt3p, lethal phenotype, glycosylation change detected
T537S
mutant of subunit Stt3p, normal growth phenotype, glycosylation change detected
T541A
mutant of subunit Stt3p, extremely temperature-sensitive phenotype, glycosylation change detected
T541S
mutant of subunit Stt3p, normal growth phenotype, glycosylation change detected
additional information
N60Q
mutant of subunit Stt3p, mutant of subunit Stt3p, normal growth phenotype, no glycosylation change detected
N60Q
mutant of subunit Wbp1p, normal growth phenotype, glycosylation change detected
additional information
mutation of the active-site cysteine residues of Ost6p and its paralogue Ost3p affect the glycosylation efficiency of a subset of glycosylation sites
additional information
-
mutation of the active-site cysteine residues of Ost6p and its paralogue Ost3p affect the glycosylation efficiency of a subset of glycosylation sites
additional information
-
strains with deleted OST3 and OST6 loci are grown with plasmids introducing either one of the subunits
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54
-
absolute melting temperature of large soluble domain of the subunit Nlt1p
65
-
absolute melting temperature of large soluble domain of the subunit Swp1p
73
-
absolute melting temperature of large soluble domain of the subunit Wbp1p
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
DAD1 might provide structural and functional integrity for the OST complex
-
strongly stabilized by addition of phospholipids upon detergent solubilization, phosphatidylcholine is twice as effective as phosphatidylethanolamine
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, Nonidet-solubilized crude enzyme, 25% glycerol, 0.01% 2-mercaptoethanol, 18% loss of activity after 1 month and 87% after 5 months
-
-70°C, Nonidet-solubilized crude enzyme, 25% glycerol, 0.01% 2-mercaptoethanol, retains 90% of original activity after 1 month and 55% after 5 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity purification of a tagged Stt3 protein (component of the oligosaccharyltransferase complex)
dissolution in denaturing buffer (6 M guanidine hydrochloride, 500 mM Na Cl, 25 mM imidazole, 20 mM phosphate buffer, pH 7.4), cenrtrifugation, supernatant loaded onto nickel-NTA column for affinity chromatography with 20 mM phosphate buffer, pH 6.5, SDS-PAGE
purification of an affinity-tagged version of the enzyme complex from a membrane protein fraction
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
subcloning, overexpression, and a method of production of the pure C-terminal domain of Stt3p at 60-70 mg/l in Escherichia coli
creation of a yeast strain in which the essential 64000 Da glycoprotein Nlt1p subunit of the oligosaccharyl transferase is modified by the addition of a 22-residue carboxy-terminal affinity tag, the tag includes both an 8-residue FLAG epitope and a 6-residue histidine motif
-
PCR-amplification, expression of the pure C-terminal domain of the subunit Stt3p in Escherichia coli BL21 (DE3)
plasmids with subunit genes introduced into mutants lacking both subunits
-
replacement of Saccharomyces cerevisiae Stt3p by the Trypanosoma cruzi homologue
-
the large soluble domains of the subunits Nlt1p, Swp1p and Wbp1p are expressed in a baculovirus-infected insect cell system
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kaplan, H.A.; Welply, J.K.; Lennarz, W.J.
Oligosaccharyl transferase: the central enzyme in the pathway of glycoprotein assembly
Biochim. Biophys. Acta
906
161-173
1987
Saccharomyces cerevisiae, Canis lupus familiaris, Gallus gallus, Oryctolagus cuniculus, Drosophila melanogaster, Mus musculus, Rattus norvegicus
Lee, J.; Coward, J.K.
Oligosaccharyltransferase: synthesis and use of deuterium-labeled peptide substrates as mechanistic probes
Biochemistry
32
6794-6801
1993
Saccharomyces cerevisiae
Bosch, M.; Trombetta, S.; Engstrom, U.; Parodi, A.J.
Characterization of dolichol diphosphate oligosaccharide: protein oligosaccharyltransferase and glycoprotein-processing glucosidases occurring in trypanosomatid protozoa
J. Biol. Chem.
263
17360-17365
1988
Crithidia fasciculata, Leptomonas samueli, Rattus norvegicus, Saccharomyces cerevisiae, Strigomonas culicis, Trypanosoma cruzi
Sharma, C.B.; Lehle, L.; Tanner, W.
N-Glycosylation of yeast proteins. Characterization of the solubilized oligosaccharyl transferase
Eur. J. Biochem.
116
101-108
1981
Saccharomyces cerevisiae
Karaoglu, D.; Kelleher, D.J.; Gilmore, R.
Allosteric regulation provides a molecular mechanism for preferential utilization of the fully assembled dolichol-linked oligosaccharide by the yeast oligosaccharyltransferase
Biochemistry
40
12193-12206
2001
Saccharomyces cerevisiae
Karaoglu, D.; Kelleher, D.J.; Gilmore, R.
The highly conserved Stt3 protein is a subunit of the yeast oligosaccharyltransferase and forms a subcomplex with Ost3p and Ost4p
J. Biol. Chem.
272
32513-32520
1997
Saccharomyces cerevisiae
Pathak, R.; Imperiali, B.
A dual affinity tag on the 64-kDa Nlt1p subunit allows the rapid characterization of mutant yeast oligosaccharyl transferase complexes
Arch. Biochem. Biophys.
338
1-6
1997
Saccharomyces cerevisiae
Knauer, R.; Lehle, L.
The oligosaccharyltransferase complex from yeast
Biochim. Biophys. Acta
1426
259-273
1999
Canis lupus familiaris, Gallus gallus, Homo sapiens, Sus scrofa, Saccharomyces cerevisiae (P48439), Saccharomyces cerevisiae
Ufret, M.d.L.; Imperiali, B.
Probing the extended binding determinants of oligosaccharyl transferase with synthetic inhibitors of asparagine-linked glycosylation
Bioorg. Med. Chem. Lett.
10
281-284
2000
Saccharomyces cerevisiae
Dempski, R.E., Jr.; Imperiali, B.
Heterologous expression and biophysical characterization of soluble oligosaccharyl transferase subunits
Arch. Biochem. Biophys.
431
63-70
2004
Saccharomyces cerevisiae
Chavan, M.; Rekowicz, M.; Lennarz, W.
Insight into functional aspects of Stt3p, a subunit of the oligosaccharyl transferase. Evidence for interaction of the N-terminal domain of Stt3p with the protein kinase C cascade
J. Biol. Chem.
278
51441-51447
2003
Saccharomyces cerevisiae
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
Sugiura, M.; Takagi, H.
Yeast cell death caused by mutation of the OST2 gene encoding the epsilon-subunit of Saccharomyces cerevisiae oligosaccharyltransferase
Biosci. Biotechnol. Biochem.
70
1234-1241
2006
Saccharomyces cerevisiae (P46964), Saccharomyces cerevisiae
Kowarik, M.; Young, N.M.; Numao, S.; Schulz, B.L.; Hug, I.; Callewaert, N.; Mills, D.C.; Watson, D.C.; Hernandez, M.; Kelly, J.F.; Wacker, M.; Aebi, M.
Definition of the bacterial N-glycosylation site consensus sequence
EMBO J.
25
1957-1966
2006
Saccharomyces cerevisiae
Schwarz, M.; Knauer, R.; Lehle, L.
Yeast oligosaccharyltransferase consists of two functionally distinct sub-complexes, specified by either the Ost3p or Ost6p subunit
FEBS Lett.
579
6564-6568
2005
Saccharomyces cerevisiae
Kelleher, D.J.; Gilmore, R.
An evolving view of the eukaryotic oligosaccharyltransferase
Glycobiology
16
47R-62R
2006
Saccharomyces cerevisiae, Canis lupus familiaris
Chavan, M.; Yan, A.; Lennarz, W.J.
Subunits of the translocon interact with components of the oligosaccharyl transferase complex
J. Biol. Chem.
280
22917-22924
2005
Saccharomyces cerevisiae
Kelleher, D.J.; Banerjee, S.; Cura, A.J.; Samuelson, J.; Gilmore, R.
Dolichol-linked oligosaccharide selection by the oligosaccharyltransferase in protist and fungal organisms
J. Cell Biol.
177
29-37
2007
Saccharomyces cerevisiae, Cryptococcus neoformans, Entamoeba histolytica, Trichomonas vaginalis, Trypanosoma cruzi
Yan, A.; Wu, E.; Lennarz, W.J.
Studies of yeast oligosaccharyl transferase subunits using the split-ubiquitin system: topological features and in vivo interactions
Proc. Natl. Acad. Sci. USA
102
7121-7126
2005
Saccharomyces cerevisiae
Castro, O.; Movsichoff, F.; Parodi, A.J.
Preferential transfer of the complete glycan is determined by the oligosaccharyltransferase complex and not by the catalytic subunit
Proc. Natl. Acad. Sci. USA
103
14756-14760
2006
Saccharomyces cerevisiae
Chavan, M.; Chen, Z.; Li, G.; Schindelin, H.; Lennarz, W.J.; Li, H.
Dimeric organization of the yeast oligosaccharyl transferase complex
Proc. Natl. Acad. Sci. USA
103
8947-8952
2006
Saccharomyces cerevisiae
Kowarik, M.; Numao, S.; Feldman, M.F.; Schulz, B.L.; Callewaert, N.; Kiermaier, E.; Catrein, I.; Aebi, M.
N-linked glycosylation of folded proteins by the bacterial oligosaccharyltransferase
Science
314
1148-1150
2006
Saccharomyces cerevisiae
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
Li, H.; Chavan, M.; Schindelin, H.; Lennarz, W.J.; Li, H.
Structure of the oligosaccharyl transferase complex at 12.ANG. resolution
Structure
16
432-440
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae LY510-514
Huang, C.; Mohanty, S.; Banerjee, M.
A novel method of production and biophysical characterization of the catalytic domain of yeast oligosaccharyl transferase
Biochemistry
49
1115-1126
2010
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P39007)
Spirig, U.; Bodmer, D.; Wacker, M.; Burda, P.; Aebi, M.
The 3.4-kDa Ost4 protein is required for the assembly of two distinct oligosaccharyltransferase complexes in yeast
Glycobiology
15
1396-1406
2005
Saccharomyces cerevisiae
Hese, K.; Otto, C.; Routier, F.H.; Lehle, L.
The yeast oligosaccharyltransferase complex can be replaced by STT3 from Leishmania major
Glycobiology
19
160-171
2008
Leishmania major, Saccharomyces cerevisiae (P33767 and Q02791 and P39007 and P41543 and P48439), Saccharomyces cerevisiae
Nasab, F.P.; Schulz, B.L.; Gamarro, F.; Parodi, A.J.; Aebi, M.
All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiae
Mol. Biol. Cell
19
3758-3768
2008
Leishmania major, Saccharomyces cerevisiae (P33767 and Q02791 and P39007 and P41543 and P48439), Saccharomyces cerevisiae
Schulz, B.L.; Aebi, M.
Analysis of glycosylation site occupancy reveals a role for Ost3p and Ost6p in site-specific N-glycosylation efficiency
Mol. Cell. Proteomics
8
357-364
2009
Saccharomyces cerevisiae
Spirig, U.; Glavas, M.; Bodmer, D.; Reiss, G.; Burda, P.; Lippuner, V.; te Heesen, S.; Aebi, M.
The STT3 protein is a component of the yeast oligosaccharyltransferase complex
Mol. Gen. Genet.
256
628-637
1997
Saccharomyces cerevisiae (P39007), Saccharomyces cerevisiae
Schulz, B.L.; Stirnimann, C.U.; Grimshaw, J.P.; Brozzo, M.S.; Fritsch, F.; Mohorko, E.; Capitani, G.; Glockshuber, R.; Grtter, M.G.; Aebi, M.
Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency
Proc. Natl. Acad. Sci. USA
106
11061-11066
2009
Saccharomyces cerevisiae (Q03723), Saccharomyces cerevisiae
Harada, Y.; Li, H.; Li, H.; Lennarz, W.J.
Oligosaccharyltransferase directly binds to ribosome at a location near the translocon-binding site
Proc. Natl. Acad. Sci. USA
106
6945-6949
2009
Saccharomyces cerevisiae
Mohorko, E.; Glockshuber, R.; Aebi, M.
Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation
J. Inherit. Metab. Dis.
34
869-878
2011
Saccharomyces cerevisiae, Canis lupus familiaris, Homo sapiens
Jamaluddin, M.F.; Bailey, U.M.; Tan, N.Y.; Stark, A.P.; Schulz, B.L.
Polypeptide binding specificities of Saccharomyces cerevisiae oligosaccharyltransferase accessory proteins Ost3p and Ost6p
Protein Sci.
20
849-855
2011
Saccharomyces cerevisiae (P48439), Saccharomyces cerevisiae (Q03723), Saccharomyces cerevisiae
Mohanty, S.; Chaudhary, B.P.; Zoetewey, D.
Structural insight into the mechanism of N-linked glycosylation by oligosaccharyltransferase
Biomolecules
10
624
2020
Homo sapiens (P46977 AND P0C6T2 AND P61165 AND P61803 AND P04843 AND P04844 AND P39656 AND Q9NRP0), Homo sapiens (Q8TCJ2 AND P0C6T2 AND P61165 AND P61803 AND P04843 AND P04844 AND P39656 AND Q9NRP0), Homo sapiens, Saccharomyces cerevisiae (P41543 AND P46964 AND P48439 AND Q99380 AND Q92316 AND P39007 AND P33767 AND Q02795), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P41543 AND P46964 AND P48439 AND Q99380 AND Q92316 AND P39007 AND P33767 AND Q02795)
EXTERNAL LINKS (specific for EC-Number 2.4.99.18)
Transporter Classification Database (TCDB): 9.B.142.3.17, 9.B.142.3.14, 9.B.142.3.4, 9.B.142.3.5, 9.B.142.3.3
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