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Information on EC 2.4.99.18 - dolichyl-diphosphooligosaccharide-protein glycotransferase
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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
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translocon
- glc3man9glcnac2
- heptasaccharide
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s-layer
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underglycosylation
-
preassembled
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mannosyltransferases
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glycoengineering
-
hypoglycosylation
-
hetero-oligomeric
-
single-subunit
-
translocon-associated
- man9glcnac2
- lari
- drug development
- biotechnology
- medicine
- n-glycoproteins
-
glycoproteomics
- pilins
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AglB
AlgB
asparagine N-glycosyltransferase
-
-
-
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dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2
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dolichyldiphosphooligosaccharide-protein oligosaccharyltransferase
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-
-
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EC 2.4.1.119
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-
formerly
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glycosyltransferase, dolichyldiphosphooligosaccharide-protein
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-
-
-
glycosyltransferase, dolichylpyrophosphodiacetylchitobiose-protein
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-
-
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oligomannosyltransferase
-
-
-
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oligosaccharide transferase
oligosaccharyl transferase
oligosaccharyltransferase
oligosaccharyltransferase complex
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oligosaccharyltransferase, dolichyldiphosphoryloligosaccharide-protein
-
-
-
-
OST
OSTC(I)
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multiple distinct protein complexes are detected. OSTC(I) is the major complex
OTase
PglB
STT3 protein
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
AglB
archaeal homolog to bacterial PglB and eukaryotic Stt3
oligosaccharide transferase
-
-
-
-
OST
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dolichyl diphosphooligosaccharide + [protein]-L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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CAS REGISTRY NUMBER
COMMENTARY
75302-32-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
biantennary Man5GlcNAc2 dolichyl disphosphate + VSG221 coat glycoprotein
dolichyl disphosphate + ?
-
selective transfer of TbSTT3A to acidic to neutral regions of polypeptides, responsible for all paucimannose and complex N-glycans in Trypanosoma brucei glycoproteins
-
-
?
biantennary Man5GlcNAc2 dolichyl disphosphate + VSG221 coat glycoprotein
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
-
selective transfer of TbSTT3A to acidic to neutral regions of polypeptides, responsible for all paucimannose and complex N-glycans in Trypanosoma brucei glycoproteins
-
-
?
Campylobacter jejuni heptasaccharide bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
alpha-1,3-linked sugar, in vivo in Escherichia coli
-
-
?
crude lipid-linked oligosaccharide donors from Campylobacter jejuni + carboxytetramethylrhodamine-Ala-Asp-Gln-Asn-Ala-Thr-Tyr-Lys
dolichyl disphosphate + carboxytetramethylrhodamine-Ala-(oligosaccharidyl) Asp-Gln-Asp-Ala-Thr-Tyr
dolichyl diphosphooligosaccharide + Ala-Leu-Glu-Asn-Ala-Thr-Arg-NH2
?
-
-
-
-
?
dolichyl diphosphooligosaccharide + asparagine-asparagine-threonine-NH2 acceptor peptide
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
-
-
-
?
dolichyl diphosphooligosaccharide + benzoyl-Asn-Leu-Thr-N-methyl-threonine
?
-
-
-
-
?
dolichyl diphosphooligosaccharide + carboxypeptidase Y (CPY)
dolichyl disphosphate + oligosaccharidyl-(carboxypeptidase Y)
-
free enzyme
-
-
?
dolichyl diphosphooligosaccharide + diphenyl-Ala-Leu-Glu-Asn-Ala-Thr-Arg-NH2
?
-
-
-
-
?
dolichyl diphosphooligosaccharide + diphenyl-AlaLeu-Glu-Asn-Ala-Thr-Arg-NH2
?
-
-
-
-
?
dolichyl diphosphooligosaccharide + N-benzoyl-Asn-Gly-D-allo-Thr-NHCH3
?
-
-
-
-
?
dolichyl diphosphooligosaccharide + N-benzoyl-Asn-Gly-L-threo-beta-hydroxynorvaline-NHCH3
?
-
-
-
-
?
dolichyl diphosphooligosaccharide + N2-acetyl-L-asparaginyl-4-benzoyl-L-phenylalanyl-L-tyrosinamide
dolichyl diphosphate + ?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + a 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 + 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 + 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
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-L-asparagine-oligosaccharide
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
dolichyl monophosphate GlcNAc-Glc-2,3-diNAcA + [protein]-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 + Nalpha-Ac-Asn-Lys(Nepsilon-p-azidobenzoyl)-Thr-NH2
?
-
-
-
-
?
dolichyl-diphosphochitobiose-Man9Glc3 + Tyr-Asn-Leu-Thr-Ser-Val
?
-
-
-
-
?
Escherichia coli group 1 K30 capsule antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
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in vivo in Escherichia coli
-
-
?
Escherichia coli O16 antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
alpha-1,6-linked Glc with GlcNAc, in vivo in Escherichia coli
-
-
?
Escherichia coli O2 antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
rhamnose beta-1,4-linked sugar, in vivo in Escherichia coli
-
-
?
Escherichia coli O7 antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
beta-1,3-linked sugar, in vivo in Escherichia coli
-
-
?
Escherichia coli O86 antigen bound to farnesyl diphosphate + pilin
farnesyl diphosphate + glycosylated pilin
-
pentasaccharide attached to other lipid carrier, in vitro, 500 mM Tris-HCl containing 1 M sucrose and 10 mM MnCl2, pH7.5, 30°C
-
-
?
GalNAc-N,N'-diacetyl-bacillosamine-PP-undecaprenyl + acetyl-DFNAT-(4-nitrophenylalanine)-NH2
?
-
-
-
-
?
GalNAc-N,N'-diacetyl-bacillosamine-PP-undecaprenyl + acetyl-DFNVT-(4-nitrophenylalanine)-NH2
?
-
-
-
-
?
GalNAc-N,N'-diacetyl-bacillosamine-PP-undecaprenyl + acetyl-DQNAT-(4-nitrophenylalanine)-NH2
?
-
-
-
-
?
GalNAc-N,N'-diacetyl-bacillosamine-PP-undecaprenyl + acetyl-DVNAS-(4-nitrophenylalanine)-NH2
?
-
-
-
-
?
GalNAc-N,N'-diacetyl-bacillosamine-PP-undecaprenyl + acetyl-DVNAT-(4-nitrophenylalanine)-NH2
?
-
-
-
-
?
GalNAc-N,N'-diacetyl-bacillosamine-PP-undecaprenyl + acetyl-DVNVT-(4-nitrophenylalanine)-NH2
?
-
-
-
-
?
GalNAc-N,N'-diacetyl-bacillosamine-PP-undecaprenyl + acetyl-EVNAT-(4-nitrophenylalanine)-NH2
?
-
-
-
-
?
Glc3Man9GlcNAc2 dolichyl diphosphate + protein L-asparagine
?
-
-
-
-
?
Glc3Man9GlcNAc2 dolichyl disphosphate + GAYNSTSV
dolichyl disphosphate + GAY-(Glc3Man9GlcNAc2)NSTSV
-
microsomes as enzyme source, STT3-1, increase in activity from 51 to 82% when the yeast SST3 expression is turned off, when yeast SST3 is active, only slight change in activity to 103%
-
-
?
Man5GlcNAc2 dolichyl diphosphate + GAYNSTSV
dolichyl diphosphate + GAY-(Man5GlcNAc2)NSTSV
-
microsomes as enzyme source, STT3-1, increase in activity from 34 to 109% when the yeast SST3 expression is turned off, when yeast SST3 is active, increase in activity to 115%
-
-
?
Man6GlcNAc2 dolichyl diphosphate + GAYNSTSV
dolichyl diphosphate + GAY-(Man6GlcNAc2)NSTSV
-
microsomes as enzyme source, STT3-1, increase in activity from 46 to 151% when the yeast SST3 expression is turned off, when yeast SST3 is active, increase in activity to 173%
-
-
?
Man9GlcNAc2 dolichyl disphosphate + GAYNSTSV
dolichyl disphosphate + GAY-(Man9GlcNAc2)NSTSV
-
microsomes as enzyme source, STT3-1, increase in activity from 54 to 172% when the yeast SST3 expression is turned off, when yeast SST3 is active, increase in activity to 202%
-
-
?
N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol + KDFNVSKA
tritrans,heptacis-undecaprenyl diphosphate + Lys-Asp-Phe-N4-[N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-beta-D-bacillosaminyl]-Asn-Val-Ser-Lys-Ala
-
-
-
-
?
N-acetyl-D-glucosamine + glycoprotein bound to polysaccharide cell wall
?
-
glycoproteins as substrates are P15703, O13547, P53301, P32623, P28319, P38248, P22146, Q03655, Q08193, P38616
-
-
?
pentaprenyl diphospho-N-acetyl-D-galactosamine + [protein]-L-asparagine
pentaprenyl diphosphate + [protein]-N-(N-acetyl-D-galactosaminyl)-L-asparagine
PglB can utilize shorter polyisoprenol (pentaprenol) as the lipid carrier, albeit with reduced efficiency
-
-
?
peptidoglycan bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
transfer of subunit of the peptidoglycan petapeptide, no transfer of the complete peptidoglycan is observed, in vivo in Salmonella enterica
-
-
?
Pseudomonas aeruginosa O11 antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
FucNac, in vivo in Escherichia coli
-
-
?
Salmonella enterica O antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
in vivo in Escherichia coli
-
-
?
Salmonella typhimurium LT2 antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
in vivo in Escherichia coli, in vivo in Salmonella enterica serovar Typhimurium LT2 strain
-
-
?
triantennary Man9GlcNAc2 dolichyl disphosphate + VSG221 coat glycoprotein
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
-
selective transfer of TbSTT3B to neutral to basic regions of polypeptides responsible for most or all oligomannose N-glycans in Trypanosoma brucei glycoproteins
-
-
?
undecaprenyl diphospho-N-acetyl-D-galactosamine + [protein]-L-asparagine
undecaprenyl diphosphate + [protein]-N-(N-acetyl-D-galactosaminyl)-L-asparagine
PglB is solely responsible for the oligosaccharyltransferase activity. PglB can transfer a monosaccharide, e.g. GalNAc to a peptide acceptor. PglB exhibits relaxed sugar substrate specificity
-
-
?
crude lipid-linked oligosaccharide donors from Campylobacter jejuni + carboxytetramethylrhodamine-Ala-Asp-Gln-Asn-Ala-Thr-Tyr-Lys
dolichyl disphosphate + carboxytetramethylrhodamine-Ala-(oligosaccharidyl) Asp-Gln-Asp-Ala-Thr-Tyr
37°C, 50 mM Tris-HCl, pH 7.5
-
-
?
crude lipid-linked oligosaccharide donors from Campylobacter jejuni + carboxytetramethylrhodamine-Ala-Asp-Gln-Asn-Ala-Thr-Tyr-Lys
dolichyl disphosphate + carboxytetramethylrhodamine-Ala-(oligosaccharidyl) Asp-Gln-Asp-Ala-Thr-Tyr
-
37°C, 50 mM Tris-HCl, pH 7.5
-
-
?
dolichyl diphosphate-di-N-acetylchitobiose + Tyr-Asn-Leu-Thr-Ser-Val
?
-
-
-
-
?
dolichyl diphosphate-di-N-acetylchitobiose + Tyr-Asn-Leu-Thr-Ser-Val
?
-
-
-
-
?
dolichyl diphosphochitobiose-(mannosyl)9-(glucosyl)3 + synthetic hexapeptide
?
-
-
-
-
?
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 + N2-acetyl-L-asparaginyl-4-benzoyl-L-phenylalanyl-L-tyrosinamide
dolichyl diphosphate + ?
-
-
-
-
?
dolichyl diphosphooligosaccharide + N2-acetyl-L-asparaginyl-4-benzoyl-L-phenylalanyl-L-tyrosinamide
dolichyl diphosphate + ?
-
-
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine
-
DQNAT is the optimal acceptor substrate. PglB is not capable of utilizing glycosyl donors such as dolichyl-pyrophosphatechitobiose
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine
-
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 + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine
-
ribophorin I can regulate the delivery of precursor proteins to the oligosaccharyltransferase complex by capturing substrates and presenting them to the catalytic core
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine
-
PglL is able to transfer diverse oligo- and polysaccharides
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine
-
PilO activity is restricted to short oligosaccharides
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine
-
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 + 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
-
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 + 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
-
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 + 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
-
reaction with oligosaccharide-lipid present in hen oviduct microsomes and Nalpha-Ac-Asn-Leu-Thr-NHCH3. Kinetic study with intact microsomal membrane
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
-
Asn-Xaa-Thr/Ser is a necessary and sufficient prerequisite for N-glycosylation
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
-
(Glc)n-(Man)x-GlcNAc2-diphosphoryldolichol as oligosaccharyl donor and tryptic peptide consisting of residues 29-59 from bovine alpha-lactalbumin as acceptor
-
?
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
-
peptide acceptor specificity
-
?
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 + 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
-
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 + 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 + 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
-
Asn-Xaa-Thr/Ser is a necessary and sufficient prerequisite for N-glycosylation
-
?
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
-
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 + 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 + 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
-
highly stereospecific for the conformation of the 3-carbon atom in the hydroxy amino acid. Binding of the threonine beta-methyl group by the enzyme is also specific, with serine, L-threo-beta-hydroxynorvaline and L-beta-hydroxynorleucine containing tripeptides all bound less efficiently than the threonine CH3-CH(OH) group
-
?
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
-
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 + 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
-
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 + 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 disphosphate + protein with oligosaccharide attached to protein L-asparagine
-
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
-
-
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
-
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
-
-
-
-
?
dolichyl diphosphooligosaccharide + synthetic tripeptides
?
-
Asn-Tyr-Thr
-
-
?
dolichyl diphosphooligosaccharide + synthetic tripeptides
?
-
no substrates are Asn-Leu-Thr-derivatives containing asparagine modifications or substitution
-
-
?
dolichyl diphosphooligosaccharide + synthetic tripeptides
?
-
peptide hydrophobicity increases its acceptor activity
-
-
?
dolichyl diphosphooligosaccharide + synthetic tripeptides
?
-
Asn-Leu-Thr and its N-terminal acetyl-, benzoyl-, octanoyl- or t-butoxycarbonyl-derivatives
-
-
?
dolichyl diphosphooligosaccharide + synthetic tripeptides
?
-
Ac-Asn-Leu-Thr-NH2, Ac-Asn-Ala-Thr-NH2 and benzoyl-Asn-Leu-N-methylamide
-
-
?
dolichyl diphosphooligosaccharide + synthetic tripeptides
?
-
peptides that serve as acceptors show a secondary structural motif that involves the interaction between the asparagine side-chain carboxamide and the backbone amide of the threonine
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + 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 + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
despite processing distinct lipid-linked glycans in their native hosts, AglB from Haloarcula marismortui can readily replace their counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of aglB
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
haloarchaeal AglB proteins display substrate promiscuity. Haloferax volcanii, Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei AglB each contain distinct glycan-charged lipid carriers. Haloferax volcanii can be functionally replaced by its haloarchaeal homologues
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + 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 + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
despite processing distinct lipid-linked glycans in their native hosts, AglB from Halobacterium salinarum can readily replace their counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of aglB
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
haloarchaeal AglB proteins display substrate promiscuity. Haloferax volcanii, Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei AglB each contain distinct glycan-charged lipid carriers. Haloferax volcanii can be functionally replaced by its haloarchaeal homologues
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + 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 + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
despite processing distinct lipid-linked glycans in their native hosts, AglB from Haloferax mediterranei can readily replace their counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of aglB
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
haloarchaeal AglB proteins display substrate promiscuity. Haloferax volcanii, Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei AglB each contain distinct glycan-charged lipid carriers. Haloferax volcanii can be functionally replaced by its haloarchaeal homologues
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + 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 + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
despite processing distinct lipid-linked glycans in their native hosts, AglB from Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei can readily replace their counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of aglB
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
haloarchaeal AglB proteins display substrate promiscuity. Haloferax volcanii, Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei AglB each contain distinct glycan-charged lipid carriers. Haloferax volcanii can be functionally replaced by its haloarchaeal homologues
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + 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 + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
despite processing distinct lipid-linked glycans in their native hosts, AglB from Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei can readily replace their counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of aglB
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
haloarchaeal AglB proteins display substrate promiscuity. Haloferax volcanii, Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei AglB each contain distinct glycan-charged lipid carriers. Haloferax volcanii can be functionally replaced by its haloarchaeal homologues
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + 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
-
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]-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 pyrophosphate 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, modeling, 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]-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]-L-asparagine-oligosaccharide
i.e. substrate peptide LLO prepared from Pyrococcus furiosus cells and a substrate peptide, TAMRAAla-Pro-Tyr-Asn-Val-Thr-Lys-Arg, which is optimized by peptide library experiments
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine, product analysis by mass spectrometry
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-L-asparagine-oligosaccharide
i.e. substrate peptide LLO prepared from Pyrococcus furiosus cells and a substrate peptide, TAMRAAla-Pro-Tyr-Asn-Val-Thr-Lys-Arg, which is optimized by peptide library experiments
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine, product analysis by mass spectrometry
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
-
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
PglB, the key enzyme of the Campylobacter jejuni N-glycosylation system, transfers O polysaccharide from a lipid carrier (undecaprenyl pyrophosphate) to an accept or protein. PglB is the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
PglB has relaxed specificity toward its lipid-linked glycan substrate. It can transfer its endogenous substrate, the heptasaccharide Glc(GalNAc)5Bac of Campylobacter jejuni, as well as different O antigen polysaccharides that are assembled by the rhamnosyltransferase (polymerase)-dependent mechanism on the lipid carrier undecaprenyl diphosphate
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
to investigate the substrate specificity of PglB, the transfer of a set of lipid-linked polysaccharides in Escherichia coli and Salmonella enterica serovar typhimurium is tested. A hexose linked to the C-6 of the monosaccharide at the reducing end does not inhibit the transfer of the O antigen to the acceptor protein. PglB requires an acetamido group at the C-2. A model for the mechanism of PglB involving this functional group is proposed. Eukaryotic and prokaryotic OTases catalyze the transfer of oligosaccharides by a conserved mechanism. Substitution at the C-6 position in the reducing end of the oligosaccharide does not prevent its PglB-mediated transfer to the protein acceptor AcrA. PglB transferrs a polysaccharide that is assembled by a Wzy-protein-independent pathway. An N-acetyl group in position 2 of the sugar directly linked to the undecaprenyl diphosphate carrier is necessary for recognition and/or catalysis
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
-
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
model glycoprotein carboxypeptidase Y. STT3 from Leishmania is able to complement stt3 deficiency in yeast during vegetative growth, but only poorly during sporulation. Transfers efficiently shortened lipid-linked-mannose oligosaccharides. The Leishmania STT3 homolog is functional mainly as a free enzyme with a broad specificity for the glycosyl donor. When incorporated into the OST complex, it accepts the common Glc3Man9GlcNAc2-PP-Dol donor. Three out of the four STT3 paralogs are able to functionally complement not only an stt3 mutant but also ost1, ost2, wbp1, or swp1 mutants
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
various LmOTases have different protein substrate affinities when expressed in yeast. Biosynthetic intermediates as well as the complete Glc3Man9GlcNAc2 oligosaccharide are transferred efficiently to protein by the LmSTT3D OTase isoform without any apparent substrate specificity
-
-
?
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
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 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
-
-
?
dolichyl-diphosphochitobiose-Man7Glc3 + protein-L-asparagine
?
-
-
-
-
?
dolichyl-diphosphochitobiose-Man9Glc3 + protein-L-asparagine
?
-
-
-
-
?
dolichyl-diphosphochitobiose-Man9Glc3 + protein-L-asparagine
?
-
-
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
-
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in the pathway of glycoprotein assembly
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in synthesis of N-linked glycoproteins
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
the DAD1 subunit is a defender against apoptotic cell death
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in the pathway of glycoprotein assembly
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in the pathway of glycoprotein assembly
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in synthesis of N-linked glycoproteins
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in the pathway of glycoprotein assembly
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in the pathway of glycoprotein assembly
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in the pathway of glycoprotein assembly
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
the STT3a subunit isoform mediates specific protein glycosylation steps that are necessary for cell cycle progression during osmotic stres adaption
-
-
?
additional information
?
-
-
salt stress caused growth inhibition, aberrant root-tip morphology, and callose accumulation in cgl1, is observed in an ER oligosaccharyltransferase mutant, staurosporin and temperature sensitive 3a
-
-
?
additional information
?
-
a set of peptides, TAMRA-Gly-X-X-X-Val-Thr-NH2, where the X-X-X sequence is varied for testing the N-glycosylation dependency, is validated as substrates
-
-
?
additional information
?
-
-
a set of peptides, TAMRA-Gly-X-X-X-Val-Thr-NH2, where the X-X-X sequence is varied for testing the N-glycosylation dependency, is validated as substrates
-
-
?
additional information
?
-
a set of peptides, TAMRA-Gly-X-X-X-Val-Thr-NH2, where the X-X-X sequence is varied for testing the N-glycosylation dependency, is validated as substrates
-
-
?
additional information
?
-
-
key enzyme of Campylobacter jejuni N-glycosylation system, transfers O-polysaccharides from a lipid carrier (undecaprenyl pyrophosphate) to an acceptor protein. PglB is the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer
-
-
?
additional information
?
-
-
PglB can transfer diverse oligosaccharides and polysaccharides from Escherichia coli and Pseudomonas aeruginosa to proteins, in addition to the Campylobacter jejuni glycan. PglB attaches O7 polysaccharides and Campylobacter jejuni oligosaccharides to the same Asn residue in AcrA
-
-
?
additional information
?
-
-
PglB transfers a wide variety of saccharides
-
-
?
additional information
?
-
-
no activity with acetyl-NVAAT-(para-nitrophenylalanine)-NH2 and acetyl-DVAAT-(para-nitrophenylalanine)-NH2
-
-
?
additional information
?
-
-
deletion of stt3, the only component of the oligosaccharide transferase complex detected in archaea, does not affect cell viability, it appears that N-glycosylation is not essential in Haloferax volcanii
-
-
?
additional information
?
-
-
the transcription of aglB, aglF, aglG and aglI is regulated in a coordinated manner
-
-
?
additional information
?
-
the PglB1-dependent N-glycosylation with a linear pentasaccharide requires an acidic residue at the -2 position of the N-glycosylation sequon
-
-
?
additional information
?
-
-
the PglB1-dependent N-glycosylation with a linear pentasaccharide requires an acidic residue at the -2 position of the N-glycosylation sequon
-
-
?
additional information
?
-
-
fine regulation of OTase activity is essential for normal cognitive-function development
-
-
?
additional information
?
-
-
minimal activity with alpha-linked dolichyl monophosphate N-acetylglucosamine and no glycosylation activity with peptide Ac(YKYQESSYKpNF)NH2
-
-
?
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
-
-
?
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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
Campylobacter jejuni heptasaccharide bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
alpha-1,3-linked sugar, in vivo in Escherichia coli
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + 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
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
Escherichia coli group 1 K30 capsule antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
in vivo in Escherichia coli
-
-
?
Escherichia coli O16 antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
alpha-1,6-linked Glc with GlcNAc, in vivo in Escherichia coli
-
-
?
Escherichia coli O2 antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
rhamnose beta-1,4-linked sugar, in vivo in Escherichia coli
-
-
?
Escherichia coli O7 antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
beta-1,3-linked sugar, in vivo in Escherichia coli
-
-
?
Escherichia coli O86 antigen bound to farnesyl diphosphate + pilin
farnesyl diphosphate + glycosylated pilin
-
pentasaccharide attached to other lipid carrier, in vitro, 500 mM Tris-HCl containing 1 M sucrose and 10 mM MnCl2, pH7.5, 30°C
-
-
?
N-acetyl-D-glucosamine + glycoprotein bound to polysaccharide cell wall
?
-
glycoproteins as substrates are P15703, O13547, P53301, P32623, P28319, P38248, P22146, Q03655, Q08193, P38616
-
-
?
peptidoglycan bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
transfer of subunit of the peptidoglycan petapeptide, no transfer of the complete peptidoglycan is observed, in vivo in Salmonella enterica
-
-
?
Pseudomonas aeruginosa O11 antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
FucNac, in vivo in Escherichia coli
-
-
?
Salmonella enterica O antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
in vivo in Escherichia coli
-
-
?
Salmonella typhimurium LT2 antigen bound to undecaprenyl diphosphate + pilin
undecaprenyl diphosphate + glycosylated pilin
-
in vivo in Escherichia coli, in vivo in Salmonella enterica serovar Typhimurium LT2 strain
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
-
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
-
-
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
-
-
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine
dolichyl disphosphate + protein with oligosaccharide attached to protein L-asparagine
-
-
-
-
?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
dolichyl diphosphate + 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 + 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 + 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 + 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 + 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 + 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
-
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]-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 pyrophosphate 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, modeling, 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]-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
-
PglB, the key enzyme of the Campylobacter jejuni N-glycosylation system, transfers O polysaccharide from a lipid carrier (undecaprenyl pyrophosphate) to an accept or protein. PglB is the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer
-
-
?
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
-
-
-
?
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
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 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
?
-
-
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in the pathway of glycoprotein assembly
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in synthesis of N-linked glycoproteins
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
the DAD1 subunit is a defender against apoptotic cell death
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in the pathway of glycoprotein assembly
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in the pathway of glycoprotein assembly
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in synthesis of N-linked glycoproteins
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in the pathway of glycoprotein assembly
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in the pathway of glycoprotein assembly
-
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain
?
-
central enzyme in the pathway of glycoprotein assembly
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
the STT3a subunit isoform mediates specific protein glycosylation steps that are necessary for cell cycle progression during osmotic stres adaption
-
-
?
additional information
?
-
-
salt stress caused growth inhibition, aberrant root-tip morphology, and callose accumulation in cgl1, is observed in an ER oligosaccharyltransferase mutant, staurosporin and temperature sensitive 3a
-
-
?
additional information
?
-
-
key enzyme of Campylobacter jejuni N-glycosylation system, transfers O-polysaccharides from a lipid carrier (undecaprenyl pyrophosphate) to an acceptor protein. PglB is the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer
-
-
?
additional information
?
-
-
PglB transfers a wide variety of saccharides
-
-
?
additional information
?
-
-
deletion of stt3, the only component of the oligosaccharide transferase complex detected in archaea, does not affect cell viability, it appears that N-glycosylation is not essential in Haloferax volcanii
-
-
?
additional information
?
-
-
fine regulation of OTase activity is essential for normal cognitive-function development
-
-
?
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mg2+
-
absolute requirement for a divalent cation, Mg2+ is 30% as effective as 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+
-
the enzyme requires the addition of divalent metal cations such as Mn2+
Mn2+
absolute requirement for divalent cations that can adopt an octahedral coordination geometry with preference for Mn2+ over Mg2+
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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
-
-
N-dinitrobenzoyl-Arg-Asn-Ala-epoxyethylglycine-Ala-Val
-
Asn residue of the inhibitor is glycosylated during inactivation
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
DAD1 might provide structural and functional integrity for the OST complex
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Role of the Sec14-like domain of Dbl family exchange factors in the regulation of Rho family GTPases in different subcellular sites.
Congenital Disorders of Glycosylation
Mutations in STT3A and STT3B cause two congenital disorders of glycosylation.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Mutations in STT3A and STT3B cause two congenital disorders of glycosylation.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Oligosaccharyltransferase complex-congenital disorders of glycosylation: A novel congenital disorder of glycosylation.
Dengue
Dengue Virus Hijacks a Noncanonical Oxidoreductase Function of a Cellular Oligosaccharyltransferase Complex.
Dengue
The major oligosaccharyl transferase complex genes are not involved in dengue virus replication in Aedes aegypti mosquitoes.
Epilepsies, Partial
Oligosaccharyltransferase complex-congenital disorders of glycosylation: A novel congenital disorder of glycosylation.
Glioma
Oligosaccharyltransferase inhibition Reduces Receptor Tyrosine Kinase Activation and Enhances Glioma Radiosensitivity.
Heart Defects, Congenital
Oligosaccharyltransferase complex-congenital disorders of glycosylation: A novel congenital disorder of glycosylation.
Infections
Dengue Virus Hijacks a Noncanonical Oxidoreductase Function of a Cellular Oligosaccharyltransferase Complex.
Leukemia
Identification of differentially expressed genes following treatment of monkey kidney cells with the mycotoxin fumonisin B(1).
Lung Neoplasms
Oligosaccharyltransferase Inhibition Overcomes Therapeutic Resistance to EGFR Tyrosine Kinase Inhibitors.
Microcephaly
Oligosaccharyltransferase complex-congenital disorders of glycosylation: A novel congenital disorder of glycosylation.
Neoplasms
Identification of differentially expressed genes following treatment of monkey kidney cells with the mycotoxin fumonisin B(1).
Neoplasms
Oligosaccharyltransferase inhibition induces senescence in RTK-driven tumor cells.
Neoplasms
Oligosaccharyltransferase Inhibition Overcomes Therapeutic Resistance to EGFR Tyrosine Kinase Inhibitors.
Neuronal Ceroid-Lipofuscinoses
Dolichyl-pyrophosphoryloligosaccharide protein oligosaccharide transferase in neuronal ceroid-lipofuscinosis.
Ovarian Neoplasms
Loss of the oligosaccharyl transferase subunit TUSC3 promotes proliferation and migration of ovarian cancer cells.
Spasms, Infantile
Oligosaccharyltransferase complex-congenital disorders of glycosylation: A novel congenital disorder of glycosylation.
Trypanosomiasis, African
Single-subunit oligosaccharyltransferases of Trypanosoma brucei display different and predictable peptide acceptor specificities.
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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
-
kinetic study with intact microsomal membrane. Km-value for Nalpha-Ac-Asn-Leu-Thr-NHCH3 is 0.01 mM
-
additional information
additional information
-
dissociation constant KD=9.97 mM
-
additional information
additional information
dissociation constant KD=9.97 mM
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
development of an in vitro assay, which uses polyacrylamide gel electrophoresis as the separation mechanism. The peptide substrate is labeled with a fluorescent dye, and the glycopeptide products are detected and quantified by fluorescence gel imaging. This method will is efficient and user-friendly
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
pH 6.0: about 30% of maximal activity, pH 8.0: about 20% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
P41543: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 1, P46964: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 2, P48439: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 3, Q99380: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 4, Q92316: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 5, P39007: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit STT3 (catalytic subunit), P33767: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit WBP1, Q02795: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit SWP1
SwissProt
brenda
putative oligosaccharyltransferase
UniProt
brenda
oligosaccharyltransferase A complex (catalytic subunit). P46977: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit STT3A. P0C6T2: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 4, P61165: transmembrane protein 258, P61803: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit DAD1, P04843: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 1, P04844: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 2, P39656: dolichyl-diphosphooligosaccharide-protein glycosyltransferase 48 kDa subunit, Q9NRP0: oligosaccharyltransferase complex subunit OSTC
P46977; P0C6T2; P61165; P61803; P04843; P04844; P39656; Q9NRP0
SwissProt
brenda
oligosaccharyltransferase B complex. Q8TCJ2: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit STT3B (catalytic subunit). P0C6T2: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 4, P61165: transmembrane protein 258, P61803: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit DAD1, P04843: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 1, P04844: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 2, P39656: dolichyl-diphosphooligosaccharide-protein glycosyltransferase 48 kDa subunit, Q9NRP0: oligosaccharyltransferase complex subunit OSTC
Q8TCJ2; P0C6T2; P61165; P61803; P04843; P04844; P39656; Q9NRP0
SwissProt
brenda
-
-
-
brenda
-
SwissProt
brenda
dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit OST6
SwissProt
brenda
dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit STT3
SwissProt
brenda
P41543: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 1, P46964: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 2, P48439: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 3, Q99380: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 4, Q92316: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit 5, P39007: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit STT3 (catalytic subunit), P33767: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit WBP1, Q02795: dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit SWP1
SwissProt
brenda
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 (P33767 (SwissProt)), Swp1 (Q02795 (SwissProt)), Stt3 (P39007 (SwissProt)), Ost1 (P41543 (SwissProt)), Ost2 (P46964 (SwissProt)), Ost3 (P48439 (SwissProt)), Ost4 (Q99380 (SwissProt)), Ost5, and Ost6
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
TbSTT3A transcribed in the bloodstream nor procyclic form
brenda
additional information
-
TbSTT3B transcribed in the bloodstream nor procyclic form
brenda
additional information
-
TbSTT3C not transcribed in the bloodstream nor procyclic form
brenda
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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
brenda
P46977; P0C6T2; P61165; P61803; P04843; P04844; P39656; Q9NRP0, Q8TCJ2; P0C6T2; P61165; P61803; P04843; P04844; P39656; Q9NRP0
N-linked glycosylation occurs in the endoplasmic reticulum lumen by the membrane associated oligosaccharyltransferase enzyme complex
brenda
-
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
brenda
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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
brenda
N-linked glycosylation occurs in the endoplasmic reticulum lumen by the membrane associated oligosaccharyltransferase enzyme complex
brenda
-
N-linked glycosylation occurs in the endoplasmic reticulum lumen by the membrane associated oligosaccharyltransferase enzyme complex
-
brenda
-
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
-
brenda
-
OST48, ribophorin I and ribophorin II possess a type I membrane topology with the bulk of their polypeptide chains directed to towards the lumen of the endoplasmic reticulum
brenda
reaction takes place in the lumen
brenda
PglB possesses 11 transmembrane segments and two relatively large periplasmic regions other than the C-terminal domain
brenda
-
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
brenda
-
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
brenda
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments
brenda
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. Ost4p is a minimembrane protein
brenda
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. Ost5p is a membrane protein
brenda
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
brenda
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
brenda
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
brenda
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
brenda
-
OST48, ribophorin I and ribophorin II possess a type I membrane topolyogy with the bulk of their polypeptide chains directed towards the lumen of the endoplasmic reticulum
brenda
-
integral membrane protein, tightly associated to luminal side of membrane
brenda
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ribophorin I and II are integral membrane glycoproteins
brenda
-
integral membrane protein, tightly associated to luminal side of membrane
brenda
-
integral membrane protein, tightly associated to luminal side of membrane
brenda
-
the enzyme is oriented at the luminal face of the endoplasmic membrane
brenda
-
integral membrane protein, tightly associated to luminal side of membrane
brenda
-
integral membrane protein, tightly associated to luminal side of membrane
brenda
-
integral membrane protein, tightly associated to luminal side of membrane
brenda
-
integral membrane protein, tightly associated to luminal side of membrane
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
OST is a heterooligomeric membrane protein complex in animals, plants, and fungi. In bacteria, archaea, and protozoa, OST is a monomer
evolution
-
OST is a heterooligomeric membrane protein complex in animals, plants, and fungi. In bacteria, archaea, and protozoa, OST is a monomer
evolution
-
OST is a heterooligomeric membrane protein complex in animals, plants, and fungi. In bacteria, archaea, and protozoa, OST is a monomer
evolution
the catalytic subunit of OST is called STT3 in eukaryotes, AglB in archaea, and PglB in eubacteria. Archaeoglobus f ulgidus encodes three AglB paralogues, two of them are the shortest AglBs across all domains of life.
evolution
-
the catalytic subunit of OST is called STT3 in eukaryotes, AglB in archaea, and PglB in eubacteria. Archaeoglobus f ulgidus encodes three AglB paralogues, two of them are the shortest AglBs across all domains of life.
-
malfunction
congenital disorders of glycosylation (CDG) have severe effects in humans, complete loss is lethal for eukaryots
malfunction
-
simultaneous TbSTT3A and TbSTT3B knockdown prevents parasite growth in the bloodstream
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
malfunction
-
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
malfunction
-
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. It is the substrate specificity of OST that translates defects in the biosynthesis of the oligosaccharide substrate into a generalized and multisystemic deficiency observed for the different forms of human congenital disorders of glycosylation type I. Mutations in the subunit paralogues N33/Tusc3 and IAP do not yield the pleiotropic phenotypes typical for CDG type I but specifically result in nonsyndromic mental retardation
malfunction
P46977; P0C6T2; P61165; P61803; P04843; P04844; P39656; Q9NRP0, Q8TCJ2; P0C6T2; P61165; P61803; P04843; P04844; P39656; Q9NRP0
defects in N-linked glycosylation results in a class of inherited diseases known as congenital disorders of glycosylation
metabolism
-
in the central reaction of the N-linked glycosylation pathway, one of the most abundant modifications of proteins in eukaryotes, 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
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
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
-
free monomeric enzyme with broad specificity for nonglucosylated lipid-linked mannose-oligosaccharides typical for protists, incorporated in yeast enzyme complex it also transfers the common eukaryotic Glc3Man9GlcNAc2-PP-Dol donor
physiological function
N-linked glycosylation of nascent polypeptides in the lumen of the endoplasmic reticulum
physiological function
-
O-glycosylation of type IV pilins in bacteria
physiological function
-
subunits Ost3p and Ost6p are necessary for efficient glycosylation of distinct defined glycosylation sites
physiological function
-
TbSTT3A and TbSTT3B N-glycosylation together is essential for infectivity in mice
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
-
In the yeast OST complex, OST4p regulates the incorporation of the two functionally equivalent, but mutually exclusive, subunits OST3p and OST6p. 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
oligosaccharyltransferase transfers glycan to asparagine in the N-glycosylation sequon, the lysine and isoleucine residues in the DK/MI motif participate in the Ser/Thr recognition in the sequon
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
-
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. The Stt3 subunit of OST harbors the catalytic center of the enzyme, and some components of the OST complex are involved in the recognition and utilization of glycosylation sites in specific glycoproteins. The oxidoreductase activity of subunits N33/Tusc3 and IAP is required for glycosylation of a subset of proteins essential for brain development
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
physiological function
P46977; P0C6T2; P61165; P61803; P04843; P04844; P39656; Q9NRP0, Q8TCJ2; P0C6T2; P61165; P61803; P04843; P04844; P39656; Q9NRP0
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. In humans and other mammals, the oligosaccharyltransferase (OST) complex has diverged into two distinct isoforms known as OST-A and OST-B that perform distinctly different roles in N-linked glycosylation of proteins. OST-A is connected directly to the translocation channel called Sec61 in the ER membrane and scans the newly synthesized unfolded polypeptide chain emerging from the ribosome for glycosylation sites. Therefore, OST-A is responsible for the majority of N-linked glycosylation in mammals. OST-B seems to act in a proofreading role to catch glycosylation sites that OST-A misses for partially folded proteins or proteins that contain disulfide bonds
physiological function
P46977; P0C6T2; P61165; P61803; P04843; P04844; P39656; Q9NRP0, Q8TCJ2; P0C6T2; P61165; P61803; P04843; P04844; P39656; Q9NRP0
oligosaccharyltransferase (OST) catalyzes the transfer of a high-mannose glycan onto secretory proteins in the endoplasmic reticulum. Mammals express two distinct oligosaccharyltransferase complexes that act in a cotranslational (OST-A) or posttranslocational (OST-B) manner. The distinct functions of the two human complexes are based on structural differences of their catalytic subunits STT3A and STT3B, which result in interactions with distinct subunits and different affinities for acceptor peptides
physiological function
-
oligosaccharyltransferase transfers glycan to asparagine in the N-glycosylation sequon, the lysine and isoleucine residues in the DK/MI motif participate in the Ser/Thr recognition in the sequon
-
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
-
OST complexes containing Stt3-B are more active than OST complexes harboring Stt3-A. 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
Show AA Sequence and Transmembrane Helices (7433 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16000
180000
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
48000
480000
48900
-
x * 48900, OST48, + x * 68700, ribophorin I, + x * 69300, ribophorin II + ?, calculation from nucleotide sequence
500000
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
68700
-
x * 48900, OST48, + x * 68700, ribophorin I, + x * 69300, ribophorin II + ?, calculation from nucleotide sequence
69300
-
x * 48900, OST48, + x * 68700, ribophorin I, + x * 69300, ribophorin II + ?, calculation from nucleotide sequence
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
80000
92000
-
recombinant monomeric Leishmania major SST3 enzyme with FLAG-tag, calculated and confirmed by 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
180000
-
recombinant Leishmania major SST3 with FLAG-tag, BN-PAGE probed with anti-FLAG antiserum
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
480000
oligosaccharyltransferase complex, native polyacrylamide gel electrophoresis
480000
-
recombinant Leishmania major SST3 (with exception of SST3-3) incorporated in the yeast oligosaccharyltransferase complex when native yeast SST3 is not expressed, BN-PAGE
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heptamer
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
?
-
x * 48900, OST48, + x * 68700, ribophorin I, + x * 69300, ribophorin II + ?, calculation from nucleotide sequence
heptamer
-
heteromeric OST complex comprising seven subunits, Stt3 proteins are the catalytic subunits of eukaryotic OST complexes, structure-function relationships, ddetailed overview. In the yeast OST complex, OST4p regulates the incorporation of the two functionally equivalent, but mutually exclusive, subunits OST3p and OST6p
heptamer
-
the heptameric human OST complex contains the subunits ribophorin I (OST1p), ribophorin II (Swp1p), OST48 (Wbp1p), OST4 (OST4), Stt3-A/Stt3-B (Stt3p), N33/Tusc3 and IAP (OST3p and OST6p), and DAD1 (OST2p), struccture-function relationships, Stt3 proteins are the catalytic subunits of eukaryotic OST complexes, detailed overview. Human OST4 contains a very short luminal segment with one transmembrane span followed by a cytoplasmic part consisting of approximately ten residues
heptamer
-
the human Ost4 protein contains 37 amino acids, i.e. MITDVQLAIFANMLGVSLFLLVVLYHYVAVNNPKKQE, Ost4 is a small membrane protein and belongs to one of the seven subunits of human OST, structure analysis by NMR spectroscopy, residues 5-30 adopt an alpha-helical structure, and a kink structure in the transmembrane domain may be important for its function, overview
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
additional information
Archaeoglobus AglB lacks a beta-barrel-like structure found in other AglBs and PglBs,but AglB contains a kinked helix bearing a conserved motif, called DK/MI motif, it is a variant type of the DK motif with the insertion, this particular type of the DK motif contributes to the activity. Structure comparisons, overview
additional information
-
Archaeoglobus AglB lacks a beta-barrel-like structure found in other AglBs and PglBs,but AglB contains a kinked helix bearing a conserved motif, called DK/MI motif, it is a variant type of the DK motif with the insertion, this particular type of the DK motif contributes to the activity. Structure comparisons, overview
additional information
-
Archaeoglobus AglB lacks a beta-barrel-like structure found in other AglBs and PglBs,but AglB contains a kinked helix bearing a conserved motif, called DK/MI motif, it is a variant type of the DK motif with the insertion, this particular type of the DK motif contributes to the activity. Structure comparisons, overview
-
additional information
-
oligosaccharyltransferase activity is mediated by a protein complex composed of ribophorin I, 66000 Da, and ribophorin II, 63000 Da, and a 48000 Da protein
additional information
-
the 12500 Da DAD1 protein is a tightly associated subunit of the OST both in intact membrane and in purified enzyme
additional information
-
multiple distinct protein complexes (OSTC(I), OSTC(II) and OSTC(III) are detected. All known mammalian OST subunits 8STT3-A, ribophorin I, ribophorin II, OST48 and DAD1) are present in all complexes and the proteins DC2 and KCP2 (keratinocyte-associated protein 2) are copurified with OST
additional information
-
subunit STT3-A is only recovered in the OST-III peak, while STT3-B subunit coelutes with OST-I and OST-II. Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. OST isoforms that incorporate STT3-B as a subunit are substantially more active and show a reduced ability to discriminate between donor substrates with different oligosaccharide structures
additional information
-
after SDS-PAGE the most active fractions contain four predominant protein bands with apparent molecular weight in the 50000 Da to 65000 Da range. N-terminal sequence analysis identifies the protein as ribophorin I, ribophorin II, and a 50000 Da homologue of Wbp1, a yeast protein essential for N-glycosylation
additional information
-
subunit STT3-A and SST3-B are both expressed in skin fibroblasts
additional information
P46977; P0C6T2; P61165; P61803; P04843; P04844; P39656; Q9NRP0
the eukaryotic oligosaccharyltransferase is a complex of multiple non-identical subunits. The human oligosaccharyltransferase complex is formed with either STT3A or STT3B, two paralogues of Stt3. Human oligosaccharyltransferase complexes, OST-A (with STT3A) and OST-B (containing STT3B)
additional information
Q8TCJ2; P0C6T2; P61165; P61803; P04843; P04844; P39656; Q9NRP0
the eukaryotic oligosaccharyltransferase is a complex of multiple non-identical subunits. The human oligosaccharyltransferase complex is formed with either STT3A or STT3B, two paralogues of Stt3. Human oligosaccharyltransferase complexes, OST-A (with STT3A) and OST-B (containing STT3B)
additional information
-
the eukaryotic oligosaccharyltransferase is a complex of multiple non-identical subunits. The human oligosaccharyltransferase complex is formed with either STT3A or STT3B, two paralogues of Stt3. Human oligosaccharyltransferase complexes, OST-A (with STT3A) and OST-B (containing STT3B)
additional information
-
subunit STT3-A and SST3-B are both expressed in lymphoma cell line CH12-LX
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
dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit STT3: 81529 Da
additional information
-
dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit STT3: 81529 Da
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
additional information
-
the eukaryotic oligosaccharyltransferase is a complex of multiple non-identical subunits. The Yeast oligosaccharyltransferase enzyme complex contains a single Stt3 subunit
-
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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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminal globular domain of the of the smallest AglB, purified recombinant wild-type and selenomethionine-labeled AgBs, sitting and hanging drop vapor diffusion methods, crystals grow from a hanging drop with a 1:1 volume ratio of the protein stock solution containing 20 mg/mL protein in 20 mM Tris buffer, pH 8.0, and the reservoir solution containing 0.1 M MES buffer, pH 6.5, and 12.5% PEG 3350, at 20°C, soaking of crystals in reservoir solution with 20% ethylene glycol added for cryoprotection, X-ray diffraction structure determination and analysis at 1.75-1.94 A resolution
sitting drop vapor diffusion method, crystal structure of the C-terminal globular domain of the AglB paralog, AglB-Long, at 1.9 A resolutions
2.8 A resolution crystal structure of the C-terminal globular domain, hanging drop method
hanging drop crystallization with 10 mM Tris-HCl, pH 8.0, and reservoir solution (0.1 M sodium cacodylate, pH 6.5, 18% polyethylene glycol 8000, 0.2 M calcium acetate, 20°C, cryoprotection with 0.1 M MES, pH 6.5, polyethylene glycol 8000, and 0.2 M calcium acetate)
2.7 A resolution crystal structure of the C-terminal soluble domain of Pyrococcus STT3
-
sitting drop vapor diffusion method, dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit OST6
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D520A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant cannot be expressed in Escherichia coli
D520N
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
D526A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant cannot be expressed in Escherichia coli
E521A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant cannot be expressed in Escherichia coli
E521Q
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
I522A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
I535A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant cannot be expressed in Escherichia coli
K531A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows similar OST activity compared to the wild-type enzyme
K531D
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
K531E
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
K531R
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
M524A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant cannot be expressed in Escherichia coli
N528A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
T518A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant cannot be expressed in Escherichia coli
T523A
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
D520A
-
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant cannot be expressed in Escherichia coli
-
D520N
-
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
-
D526A
-
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant cannot be expressed in Escherichia coli
-
E521Q
-
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
-
T523A
-
site-directed mutagensis of the AglB-S1 subunit of OST, the mutant shows reduced OST activity compared to the wild-type enzyme
-
D54A
XXD motif mutation, strongly reduced activity compared to wild-type
I571A
MI motif mutation, strongly reduced activity compared to wild-type
N53A
XXD motif mutation, about 40% activity remains compared to wild-type
S52D
XXD motif mutation, strongly reduced activity compared to wild-type
S52E
XXD motif mutation, strongly reduced activity compared to wild-type
D54A
-
XXD motif mutation, strongly reduced activity compared to wild-type
-
N53A
-
XXD motif mutation, about 40% activity remains compared to wild-type
-
G374D
-
the missense mutation lies in the second half of the N-terminal luminal domain of ribophorin II subunit, the affected patient presents a fairly mild clinical phenotype, no clear genotype-phenotype correlation for this mutation
D647A
-
mutant does not support glycosylation in vivo, no growth of yeast cells
D706A
-
mutant does not support glycosylation in vivo, no growth of yeast cells
D97A
-
mutant does not support glycosylation in vivo, no growth of yeast cells
E45E
-
reduced oligosaccharyltransferase activity, sufficient to allow growth of yeast cells
E95A
-
mutant does not support glycosylation in vivo, no growth of yeast cells
K709A
-
mutant does not support glycosylation in vivo, no growth of yeast cells
D518E
-
the four mutant STT3s forms a stable Oligosaccharyl transferase complex that has seriously impaired Oligosaccharyl transferase activity
D583A
-
the four mutant STT3s forms a stable Oligosaccharyl transferase complex that has seriously impaired Oligosaccharyl transferase activity
K586A
-
the four mutant STT3s forms a stable Oligosaccharyl transferase complex that has seriously impaired Oligosaccharyl transferase activity
K586R
-
the four mutant STT3s forms a stable Oligosaccharyl transferase complex that has seriously impaired Oligosaccharyl transferase activity
D518E
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
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
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
-
3 of the 4 STT3 Leishmania major STT3 proteins (not STT3-3) can complement stt3 deficiency in Saccharomyces cerevisiae during vegetative growth but not during sporulation, addition of osmotic stabilizer sorbitol (1 M) rescues the lethal phenotype during sporulation in rare cases, the yeast enzyme complex subunits ost1, ost2, wbp1 and swp1 can also be complemented by the 3 Leishmania major functional STT3 homologues
additional information
-
the leaky rice mutant dgl1 displays a change of matrix polysaccharides in its root cell wall, shorter root cell length, smaller root meristem and cell death in the root. The dgl1 mutation leads to a defect in N-glycosylation in the root
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
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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
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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
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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
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity purification of a tagged Stt3 protein (component of the oligosaccharyltransferase complex)
cells centrifuged, resuspended, and washed in 20 mM phosphate buffer, pH 7.2, with 0.3 M Na Cl, cells disrupted and centrifuged, membranes separated by ultracentrifugation of supernatant, resuspended in buffer with 2% Elugent and 25 mM imidazole buffer, proteins solubilized by tumbling, centrifuged, supernatant removed, Elugenat reduced to 1% or 0.5% n-dodecyl-beta-D-maltopyranoside, loaded onto Ni-nitrilotriacetic acid agarose column, elution with buffer containing 250 mM imidazole
-
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
partial
purification of an affinity-tagged version of the enzyme complex from a membrane protein fraction
-
recombinant N-terminally His6-tagged wild-type and selenomethionine-labeled AglB from Escherichia coli strain BL21 by nickel affinity chromatography and gel filtration, followed by anion exchange chromatography
sonication, centrifugation, supernatant absorbed to glutathione-Sepharose 4B resin, elution, concentration, reductive methylation, gel filtration with Superdex75 column, followed by anion exchange chromatography with a Resource Q column
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of DNA encoding the full-length AfAglB-S1 gene, expression of N-terminally His6-tagged wild-type and selenomethionine-labeled AglB in Escherichia coli strains BL21(DE3) and C43(DE3), respectively
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
-
despite processing distinct lipid-linked glycans in their native hosts, AglB from Haloarcula marismortui can readily replace their counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of aglB
-
despite processing distinct lipid-linked glycans in their native hosts, AglB from Halobacterium salinarum can readily replace their counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of aglB
-
despite processing distinct lipid-linked glycans in their native hosts, AglB from Haloferax mediterranei can readily replace their counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of aglB
-
expression in Escherichia coli
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
Lm STT3 paralogues LmSTT3A, LmSTT3B, LmSTT3C, or LmSTT3D are expressed individually in Saccharomyces cerevisiae. Three complemented the yeast stt3 deletion. LmSTT3D expression suppresses deletions of other essential OTase subunits (Wbp1p, Ost1p, Ost2p, and Swp1p). Leishmania major STT3 paralogues are active enzymes that do not incorporate into the yeast OTase complex, but instead form dimers
-
OST complex is composed of ribophorin I (Ost1p), ribophorin II (Swp1p), OST48 (Wbp1p), DAD1 (Ost2p), and an STT3 homologue
-
PCR-amplification fused to GST, expressed in Escherichia coli BL21 (DE3)pLysS
PCR-amplification, expression of histidine-tagged enzyme in Escherichia coli and Salmonella enterica strains
-
PCR-amplification, expression of the pure C-terminal domain of the subunit Stt3p in Escherichia coli BL21 (DE3)
PCR-amplification, TbSTT3A expression in Saccharomyces cerevisiae does not replace yeast SST3
-
PCR-amplification, TbSTT3B expression in Saccharomyces cerevisiae can replace yeast SST3, mild temperature-sensitive growth at 37°C, wild-type growth at 23°C
-
PCR-amplification, TbSTT3C expression in Saccharomyces cerevisiae can replace yeast SST3, severe growth defects at 23°C
-
PglB is overexpressed in Escherichia coli C43(DE3) at a level of 1 mg/L cell cultures
plasmids with subunit genes introduced into mutants lacking both subunits
-
preparation of a membrane fraction from Escherichia coli in which PglB has been overexpressed
-
replacement of Saccharomyces cerevisiae Stt3p by the Trypanosoma cruzi homologue
-
STT3 from Leishmania is able to complement stt3 deficiency in yeast during vegetative growth, but only poorly during sporulation. The Leishmania STT3 homolog is functional mainly as a free enzyme with a broad specificity for the glycosyl donor. When incorporated into the OST complex, it accepts the common Glc3Man9GlcNAc2-PP-Dol donor. Three out of the four STT3 paralogs are able to functionally complement not only an stt3 mutant but also ost1, ost2, wbp1, or swp1 mutants. STT3 from Leishmania is not incorporated into the complex and most likely functions as a monomeric enzyme
-
subcloning, overexpression, and a method of production of the pure C-terminal domain of Stt3p at 60-70 mg/l in Escherichia coli
the C-terminal domain of the STT3 protein of Pyrococcus furiosus is expressed in Escherichia coli cell BL21
the expression plasmid encoding the C-terminal soluble domain (residues 428713) is constructed by inserting a PCR product from genomic DNA (ATCC700819D) into the pGEX-6P-1 vector (GE Healthcare). The GST-fused sPglB protein is expressed by the addition of isopropyl-beta-D-thiogalactopyranoside at 37°C in the Escherichia coli BL21(DE3)pLysS strain. A structure-aided multiple sequence alignment of the STT3/PglB/AglB protein family reveals three types of oligosaccharyltransferases catalytic centers. This novel classification will provide a useful framework for understanding the enzymatic properties of the oligosaccharyltransferases enzymes from eukarya, archaea, and bacteria
the large soluble domains of the subunits Nlt1p, Swp1p and Wbp1p are expressed in a baculovirus-infected insect cell system
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
promising candidate for glycoengineering, the development of glycan-based vaccines and therapeutics
drug development
P46977; P0C6T2; P61165; P61803; P04843; P04844; P39656; Q9NRP0, Q8TCJ2; P0C6T2; P61165; P61803; P04843; P04844; P39656; Q9NRP0
cryoelectron microscopy structures of human oligosaccharyltransferase complexes OST-A and OST-B provide a basis for the design of inhibitors of N-glycosylation that modulate the maturation and activation of protein markers involved in tumor formation
medicine
medicine
-
PglB-mediated transfer of poylsaccharides might be valuable for in vivo production of O-polysaccharides-protein congugates for use as antibacterial vaccines
medicine
-
the development of powerful inhibitors of this enzyme would be valuable in the quest for antibiotics for Campylobacter jejuni-induced gastrointestinal disorders
medicine
-
mutation in OTase subunits are responsible for isolated cognitive deficit
medicine
-
enzyme inhibition could have therapeutic potential against trypanosomiasis
medicine
-
the relaxed specificity of the PglB oligosaccharyltransferase toward the glycan structure is exploited to create novel N-glycan structures containing two distinct Escherichia coli or Pseudomonas aeruginosa O antigens. PglB-mediated transfer of polysaccharides might be valuable for in vivo production of O polysaccharides-protein conjugates for use as antibacterial vaccines
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Das, R.C.; Heath, E.C.
Dolichyldiphosphoryloligosaccharide-protein oligosaccharyltransferase; solubilization, purification, and properties
Proc. Natl. Acad. Sci. USA
77
3811-3815
1980
Gallus gallus
brenda
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
brenda
Lee, J.; Coward, J.K.
Oligosaccharyltransferase: synthesis and use of deuterium-labeled peptide substrates as mechanistic probes
Biochemistry
32
6794-6801
1993
Saccharomyces cerevisiae
brenda
Bause, E.
Studies on the acceptor specificity of asparagine-N-glycosyl-transferase from rat liver
FEBS Lett.
103
296-299
1979
Rattus norvegicus
brenda
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
Strigomonas culicis, Saccharomyces cerevisiae, Crithidia fasciculata, Leptomonas samueli, Rattus norvegicus, Trypanosoma cruzi
brenda
Bause, E.
Active-site-directed inhibition of asparagine N-glycosyltransferases with epoxy-peptide derivatives
Biochem. J.
209
323-330
1983
Bos taurus
brenda
Welply, J.K.; Shenbagamurthi, P.; Naider, F.; Park, H.R.; Lennarz, W.J.
Active site-directed photoaffinity labeling and partial characterization of oligosaccharyltransferase
J. Biol. Chem.
260
6459-6465
1985
Gallus gallus
brenda
Kelleher, D.J.; Kreibich, G.; Gilmore, R.
Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kd protein
Cell
69
55-65
1992
Canis lupus familiaris
brenda
Imperiali, B.; Shannon, K.L.
Differences between Asn-Xaa-Thr-containing peptides: a comparison of solution conformation and substrate behavior with oligosaccharyltransferase
Biochemistry
30
4374-4380
1991
Sus scrofa
brenda
Welply, J.K.; Shenbagamurthi, P.; Lennarz, W.J.; Naider, F.
Substrate recognition by oligosaccharyltransferase. Studies on glycosylation of modified Asn-X-Thr/Ser tripeptides
J. Biol. Chem.
258
11856-11863
1983
Gallus gallus
brenda
Ronin, C.; Granier, C.; Caseti, C.; Bouchilloux, S.; van Rietschoten, J.
Synthetic substrates for thyroid oligosaccharide transferase. Effects of peptide chain length and modifications in the Asn-Xaa-Thr-region
Eur. J. Biochem.
118
159-164
1981
Gallus gallus
brenda
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
brenda
Bause, E.; Wesemann, M.; Bartoschek, A.; Breuer, W.
Epoxyethylglycyl peptides as inhibitors of oligosaccharyltransferase: double-labelling of the active site
Biochem. J.
322
95-102
1997
Sus scrofa
-
brenda
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
brenda
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
brenda
Kelleher, D.J.; Gilmore, R.
DAD1, the defender against apoptotic cell death, is a subunit of the mammalian oligosaccharyltransferase
Proc. Natl. Acad. Sci. USA
94
4994-4999
1997
Canis lupus familiaris
brenda
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
brenda
Kumar, V.; Heinemann, F.S.; Ozols, J.
Interleukin-2 induces N-glycosylation in T-cells: characterization of human lymphocyte oligosaccharyltransferase
Biochem. Biophys. Res. Commun.
247
524-529
1998
Homo sapiens
brenda
Hardt, B.; Aparicio, R.; Bause, E.
The oligosaccharyltransferase complex from pig liver: cDNA cloning, expression and functional characterisation
Glycoconj. J.
17
767-779
2001
Sus scrofa
brenda
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
brenda
Breuer, W.; Klein, R.A.; Hardt, B.; Bartoschek, A.; Bause, E.
Oligosaccharyltransferase is highly specific for the hydroxy amino acid in Asn-Xaa-Thr/Ser
FEBS Lett.
501
106-110
2001
Sus scrofa
brenda
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
brenda
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
brenda
Shibatani, T.; David, L.L.; McCormack, A.L.; Frueh, K.; Skach, W.R.
Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits
Biochemistry
44
5982-5992
2005
Canis lupus familiaris
brenda
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
brenda
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
brenda
Kelleher, D.J.; Karaoglu, D.; Mandon, E.C.; Gilmore, R.
Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties
Mol. Cell
12
101-111
2003
Canis lupus familiaris, Homo sapiens, Mus musculus
brenda
Koiwa, H.; Li, F.; McCully, M.G.; Mendoza, I.; Koizumi, N.; Manabe, Y.; Nakagawa, Y.; Zhu, J.; Rus, A.; Pardo, J.M.; Bressan, R.A.; Hasegawa, P.M.
The STT3a subunit isoform of the Arabidopsis oligosaccharyltransferase controls adaptive responses to salt/osmotic stress
Plant Cell
15
2273-2284
2003
Arabidopsis thaliana (Q93ZY3)
brenda
Feldman, M.F.; Wacker, M.; Hernandez, M.; Hitchen, P.G.; Marolda, C.L.; Kowarik, M.; Morris, H.R.; Dell, A.; Valvano, M.A.; Aebi, M.
Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli
Proc. Natl. Acad. Sci. USA
102
3016-3021
2005
Campylobacter jejuni
brenda
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
brenda
Glover, K.J.; Weerapana, E.; Numao, S.; Imperiali, B.
Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni
Chem. Biol.
12
1311-1315
2005
Campylobacter jejuni
brenda
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
brenda
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
brenda
Kelleher, D.J.; Gilmore, R.
An evolving view of the eukaryotic oligosaccharyltransferase
Glycobiology
16
47R-62R
2006
Saccharomyces cerevisiae, Canis lupus familiaris
brenda
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
brenda
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
brenda
Abu-Qarn, M.; Eichler, J.
Protein N-glycosylation in Archaea: defining Haloferax volcanii genes involved in S-layer glycoprotein glycosylation
Mol. Microbiol.
61
511-525
2006
Haloferax volcanii
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Igura, M.; Maita, N.; Obita, T.; Kamishikiryo, J.; Maenaka, K.; Kohda, D.
Purification, crystallization and preliminary X-ray diffraction studies of the soluble domain of the oligosaccharyltransferase STT3 subunit from the thermophilic archaeon Pyrococcus furiosus
Acta Crystallogr. Sect. F
63
798-801
2007
Pyrococcus furiosus (Q8U4D2), Pyrococcus furiosus
brenda
Molinari, F.; Foulquier, F.; Tarpey, P.S.; Morelle, W.; Boissel, S.; Teague, J.; Edkins, S.; Futreal, P.A.; Stratton, M.R.; Turner, G.; Matthijs, G.; Gecz, J.; Munnich, A.; Colleaux, L.
Oligosaccharyltransferase-subunit mutations in nonsyndromic mental retardation
Am. J. Hum. Genet.
82
1150-1157
2008
Homo sapiens
brenda
Chen, M.M.; Glover, K.J.; Imperiali, B.
From peptide to protein: comparative analysis of the substrate specificity of N-linked glycosylation in C. jejuni
Biochemistry
46
5579-5585
2007
Campylobacter jejuni
brenda
Igura, M.; Maita, N.; Kamishikiryo, J.; Yamada, M.; Obita, T.; Maenaka, K.; Kohda, D.
Structure-guided identification of a new catalytic motif of oligosaccharyltransferase
EMBO J.
27
234-243
2008
Pyrococcus furiosus
brenda
Kohda, D.; Yamada, M.; Igura, M.; Kamishikiryo, J.; Maenaka, K.
New oligosaccharyltransferase assay method
Glycobiology
17
1175-1182
2007
Pyrococcus furiosus
brenda
Faridmoayer, A.; Fentabil, M.A.; Mills, D.C.; Klassen, J.S.; Feldman, M.F.
Functional characterization of bacterial oligosaccharyltransferases involved in O-linked protein glycosylation
J. Bacteriol.
189
8088-8098
2007
Neisseria meningitidis, Pseudomonas aeruginosa
brenda
Yurist-Doutsch, S.; Abu-Qarn, M.; Battaglia, F.; Morris, H.R.; Hitchen, P.G.; Dell, A.; Eichler, J.
AglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein
Mol. Microbiol.
69
1234-1245
2008
Haloferax volcanii
brenda
Kang, J.S.; Frank, J.; Kang, C.H.; Kajiura, H.; Vikram, M.; Ueda, A.; Kim, S.; Bahk, J.D.; Triplett, B.; Fujiyama, K.; Lee, S.Y.; von Schaewen, A.; Koiwa, H.
Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus
Proc. Natl. Acad. Sci. USA
105
5933-5938
2008
Arabidopsis thaliana
brenda
Wilson, C.M.; Roebuck, Q.; High, S.
Ribophorin I regulates substrate delivery to the oligosaccharyltransferase core
Proc. Natl. Acad. Sci. USA
105
9534-9539
2008
Homo sapiens
brenda
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
brenda
Li, L.; Woodward, R.; Ding, Y.; Liu, X.W.; Yi, W.; Bhatt, V.S.; Chen, M.; Zhang, L.W.; Wang, P.G.
Overexpression and topology of bacterial oligosaccharyltransferase PglB
Biochem. Biophys. Res. Commun.
394
1069-1074
2010
Campylobacter jejuni (Q9S4V7), Campylobacter jejuni
brenda
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)
brenda
Izquierdo, L.; Schulz, B.L.; Rodrigues, J.A.; Guether, M.L.; Procter, J.B.; Barton, G.J.; Aebi, M.; Ferguson, M.A.
Distinct donor and acceptor specificities of Trypanosoma brucei oligosaccharyltransferases
EMBO J.
28
2650-2661
2009
Trypanosoma brucei
brenda
Magidovich, H.; Eichler, J.
Glycosyltransferases and oligosaccharyltransferases in Archaea: putative components of the N-glycosylation pathway in the third domain of life
FEMS Microbiol. Lett.
300
122-130
2009
no activity in Methanopyrus kandleri, no activity in Aeropyrum pernix, Methanothrix thermoacetophila (A0B8C2), Methanothrix thermoacetophila (A0B996), Pyrobaculum islandicum (A1RRM7), Thermofilum pendens (A1RXW3), Hyperthermus butylicus (A2BM28), Methanocorpusculum labreanum (A2SR78), Methanoculleus marisnigri (A3CRV9), Methanoculleus marisnigri (A3CXQ8), Staphylothermus marinus (A3DL26), Pyrobaculum calidifontis (A3MUV5), Methanococcus maripaludis C5 (A4FWA0), Pyrobaculum arsenaticum (A4WLR5), Metallosphaera sedula (A4YHQ7), Methanobrevibacter smithii (A5UL43), Methanococcus vannielii (A6UQ69), Methanococcus aeolicus (A6UWW3), Methanococcus maripaludis C7 (A6VH10), Methanoregula boonei (A7I4W0), Methanoregula boonei (A7I7L6), Ignicoccus hospitalis (A8A8E8), Caldivirga maquilingensis (A8MBU0), Nitrosopumilus maritimus (A9A114), Methanococcus maripaludis C6 (A9A9N9), Halobacterium salinarum (B0R4T2), Candidatus Korarchaeum cryptofilum (B1L5S3), Pyrobaculum neutrophilum (B1YAG2), Thermococcus onnurineus (B6YVI6), Thermococcus onnurineus (B6YVU0), Desulfurococcus amylolyticus (B8D352), Methanosphaerula palustris (B8GG73), Halorubrum lacusprofundi (B9LMS1), Methanothermobacter thermautotrophicus str. Delta H (O27660), Archaeoglobus fulgidus (O29867), Archaeoglobus fulgidus (O29918), Archaeoglobus fulgidus (O30195), Pyrococcus horikoshii (O58981), Pyrococcus horikoshii (O74088), Methanocella arvoryzae MRE50 (Q0W803), Methanocella arvoryzae MRE50 (Q0W817), Methanocella arvoryzae MRE50 (Q0W818), Methanococcoides burtonii (Q12VP3), Haloquadratum walsbyi (Q18GV3), Methanospirillum hungatei (Q2FSJ2), Methanospirillum hungatei (Q2FTM5), Methanospirillum hungatei (Q2FUP2), Methanosphaera stadtmanae (Q2NHD2), Natronomonas pharaonis (Q3IPK0), Methanosarcina barkeri (Q46FJ0), Methanosarcina barkeri (Q46FW5), Methanosarcina barkeri (Q46FW6), Sulfolobus acidocaldarius (Q4J9B4), Methanocaldococcus jannaschii (Q58920), Thermococcus kodakarensis (Q5JH70), Thermococcus kodakarensis (Q5JJ26), Haloarcula marismortui (Q5V4T7), Picrophilus torridus (Q6L0Y1), Methanococcus maripaludis S2 (Q6LXC8), Nanoarchaeum equitans (Q74MN3), Methanosarcina mazei (Q8PUW8), Methanosarcina mazei (Q8PZ47), Methanosarcina mazei (Q8PZ48), Methanosarcina acetivorans (Q8TJM6), Methanosarcina acetivorans (Q8TJM7), Methanosarcina acetivorans (Q8TJM8), Methanosarcina acetivorans (Q8TRK3), Pyrococcus furiosus (Q8U3P6), Pyrococcus furiosus (Q8U4D2), Pyrobaculum aerophilum (Q8ZTY7), Sulfurisphaera tokodaii (Q973G2), Thermoplasma volcanium (Q979C6), Saccharolobus solfataricus (Q97Z77), Thermoplasma acidophilum (Q9HJ37), Halobacterium salinarum NRC-1 (Q9HQP2), Pyrococcus abyssi (Q9UYP5), Pyrococcus abyssi (Q9UZF5), Pyrococcus abyssi (Q9V250)
brenda
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
brenda
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
brenda
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
brenda
Faridmoayer, A.; Fentabil, M.A.; Haurat, M.F.; Yi, W.; Woodward, R.; Wang, P.G.; Feldman, M.F.
Extreme substrate promiscuity of the Neisseria oligosaccharyl transferase involved in protein O-glycosylation
J. Biol. Chem.
283
34596-34604
2008
Neisseria meningitidis
brenda
Maita, N.; Nyirenda, J.; Igura, M.; Kamishikiryo, J.; Kohda, D.
Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases
J. Biol. Chem.
285
4941-4950
2010
Campylobacter jejuni (Q5HTX9), Campylobacter jejuni
brenda
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
brenda
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
brenda
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
brenda
Wacker, M.; Feldman, M.F.; Callewaert, N.; Kowarik, M.; Clarke, B.R.; Pohl, N.L.; Hernandez, M.; Vines, E.D.; Valvano, M.A.; Whitfield, C.; Aebi, M.
Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems
Proc. Natl. Acad. Sci. USA
103
7088-7093
2006
Campylobacter jejuni
brenda
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
brenda
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
brenda
Gayen, S.; Kang, C.
Solution structure of a human minimembrane protein Ost4, a subunit of the oligosaccharyltransferase complex
Biochem. Biophys. Res. Commun.
409
572-576
2011
Homo sapiens
brenda
Matsumoto, S.; Igura, M.; Nyirenda, J.; Matsumoto, M.; Yuzawa, S.; Noda, N.; Inagaki, F.; Kohda, D.
Crystal structure of the C-terminal globular domain of oligosaccharyltransferase from Archaeoglobus fulgidus at 1.75 A resolution
Biochemistry
51
4157-4166
2012
Archaeoglobus fulgidus (O29918), Archaeoglobus fulgidus, Archaeoglobus fulgidus DSM 4306 (O29918)
brenda
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
brenda
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
brenda
Matsumoto, S.; Shimada, A.; Kohda, D.
Crystal structure of the C-terminal globular domain of the third paralog of the Archaeoglobus fulgidus oligosaccharyltransferases
BMC Struct. Biol.
13
11
2013
Archaeoglobus fulgidus (O29867), Archaeoglobus fulgidus
brenda
Cohen-Rosenzweig, C.; Guan, Z.; Shaanan, B.; Eichler, J.
Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans
Appl. Environ. Microbiol.
80
486-496
2014
Haloarcula marismortui, Halobacterium salinarum, Haloferax volcanii, Haloferax mediterranei, Haloferax volcanii DSM 3757
brenda
Larkin, A.; Chang, M.M.; Whitworth, G.E.; Imperiali, B.
Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis
Nat. Chem. Biol.
9
367-373
2013
Methanococcus voltae
brenda
Qin, C.; Li, Y.; Gan, J.; Wang, W.; Zhang, H.; Liu, Y.; Wu, P.
OsDGL1, a homolog of an oligosaccharyltransferase complex subunit, is involved in N-glycosylation and root development in rice
Plant Cell Physiol.
54
129-137
2013
Oryza sativa
brenda
Mohanty, S.; Chaudhary, B.P.; Zoetewey, D.
Structural insight into the mechanism of N-linked glycosylation by oligosaccharyltransferase
Biomolecules
10
624
2020
Saccharomyces cerevisiae (P41543 AND P46964 AND P48439 AND Q99380 AND Q92316 AND P39007 AND P33767 AND Q02795), Saccharomyces cerevisiae, 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 ATCC 204508 (P41543 AND P46964 AND P48439 AND Q99380 AND Q92316 AND P39007 AND P33767 AND Q02795)
brenda
Ramirez, A.S.; Kowal, J.; Locher, K.P.
Cryo-electron microscopy structures of human oligosaccharyltransferase complexes OST-A and OST-B
Science
366
1372-1375
2019
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
brenda
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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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Release 2023.1 (January 2023)
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