2.4.99.18: dolichyl-diphosphooligosaccharide-protein glycotransferase
This is an abbreviated version!
For detailed information about dolichyl-diphosphooligosaccharide-protein glycotransferase, go to the full flat file.
Word Map on EC 2.4.99.18
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2.4.99.18
-
n-glycosylation
-
n-linked
-
glycans
-
lipid-linked
-
sequons
-
asparagine-linked
-
jejuni
-
campylobacter
-
dolichol
-
ribophorins
-
otase
-
cotranslational
-
bloc
-
dolichol-linked
-
translocon
-
glc3man9glcnac2
-
heptasaccharide
-
s-layer
-
underglycosylation
-
preassembled
-
mannosyltransferases
-
glycoengineering
-
hypoglycosylation
-
hetero-oligomeric
-
single-subunit
-
translocon-associated
-
man9glcnac2
-
lari
-
drug development
-
biotechnology
-
medicine
-
n-glycoproteins
-
glycoproteomics
-
pilins
- 2.4.99.18
-
n-glycosylation
-
n-linked
- glycans
-
lipid-linked
-
sequons
-
asparagine-linked
- jejuni
- campylobacter
- dolichol
-
ribophorins
- otase
-
cotranslational
-
bloc
-
dolichol-linked
-
translocon
- glc3man9glcnac2
- heptasaccharide
-
s-layer
-
underglycosylation
-
preassembled
-
mannosyltransferases
-
glycoengineering
-
hypoglycosylation
-
hetero-oligomeric
-
single-subunit
-
translocon-associated
- man9glcnac2
- lari
- drug development
- biotechnology
- medicine
- n-glycoproteins
-
glycoproteomics
- pilins
Reaction
Synonyms
AglB, AglB-L, AlgB, asparagine N-glycosyltransferase, DGL1, dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2, dolichyl-diphosphooligosaccharide-protein glycosyltransferase, dolichyldiphosphooligosaccharide-protein oligosaccharyltransferase, EC 2.4.1.119, glycosyltransferase, dolichyldiphosphooligosaccharide-protein, glycosyltransferase, dolichylpyrophosphodiacetylchitobiose-protein, L.m.STT3, Lm STT3, oligomannosyltransferase, oligosaccharide transferase, oligosaccharyl transferase, oligosaccharyl transferase 16 kDa subunit, oligosaccharyl transferase subunit epsilon, oligosaccharyl transferase subunit OST2, oligosaccharyltransferase, oligosaccharyltransferase complex, oligosaccharyltransferase STT3, oligosaccharyltransferase, dolichyldiphosphoryloligosaccharide-protein, OST, OST-A, OST-B, OST-I, OST-II, OST-III, OST1, OST2, OST3, Ost3p, OST4, OST5, Ost6p, OSTC(I), OSTC(II), OSTC(III), OTase, PglB, PglB oligosaccharyltransferase, PglB1, PglL, PilO, STT3, STT3 protein, STT3-1, STT3-2, STT3-3, STT3-4, Swp1p, TbSTT3A, TbSTT3B, TbSTT3C, Wbp1p, yeast oligosaccharyl transferase
ECTree
2.4.99.18 dolichyl-diphosphooligosaccharide-protein glycotransferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.4.99.18 - dolichyl-diphosphooligosaccharide-protein glycotransferase
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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
-
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
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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
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the STT3a subunit isoform mediates specific protein glycosylation steps that are necessary for cell cycle progression during osmotic stres adaption
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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
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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
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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
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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
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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
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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
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PglB transfers a wide variety of saccharides
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no activity with acetyl-NVAAT-(para-nitrophenylalanine)-NH2 and acetyl-DVAAT-(para-nitrophenylalanine)-NH2
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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
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the transcription of aglB, aglF, aglG and aglI is regulated in a coordinated manner
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the PglB1-dependent N-glycosylation with a linear pentasaccharide requires an acidic residue at the -2 position of the N-glycosylation sequon
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the PglB1-dependent N-glycosylation with a linear pentasaccharide requires an acidic residue at the -2 position of the N-glycosylation sequon
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fine regulation of OTase activity is essential for normal cognitive-function development
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minimal activity with alpha-linked dolichyl monophosphate N-acetylglucosamine and no glycosylation activity with peptide Ac(YKYQESSYKpNF)NH2
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allosteric communication between regulatory and catalytic dolichol-linked oligosaccharide binding sites
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evidence against either enol lactone or ketone formation as an intermediate
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oligosaccharyl transferase catalyzes the first committed step in N-linked protein glycosylation, a cotranslational process that occurs in the lumen of the endoplasmic reticulum
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Pkc1p cascade controls N-glycosylation by regulation of Stt3p activity
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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
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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
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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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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