2.4.99.21: dolichyl-phosphooligosaccharide-protein glycotransferase
This is an abbreviated version!
For detailed information about dolichyl-phosphooligosaccharide-protein glycotransferase, go to the full flat file.
Word Map on EC 2.4.99.21
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2.4.99.21
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cyclin-dependent
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creatine
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cystathionine
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cell-cycle
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retinoblastoma
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homocysteine
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p21cip1
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beta-synthase
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p57kip2
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homocystinuria
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ckis
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checkpoint
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d-type
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p18ink4c
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mthfr
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palbociclib
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cdk-dependent
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flavopiridol
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anaphase
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olomoucine
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e-cdk2
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cyclin-cdk
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r-roscovitine
- 2.4.99.21
-
cyclin-dependent
- creatine
- cystathionine
-
cell-cycle
-
retinoblastoma
- homocysteine
-
p21cip1
-
beta-synthase
-
p57kip2
-
homocystinuria
- ckis
-
checkpoint
-
d-type
-
p18ink4c
- mthfr
- palbociclib
-
cdk-dependent
- flavopiridol
-
anaphase
- olomoucine
-
e-cdk2
-
cyclin-cdk
-
r-roscovitine
Reaction
Synonyms
AF_0380, AglB, AglB protein, AglB-L, aglB1, AlgB, archaeal oligosaccharyl transferase, dolichyl-monophosphooligosaccharide-protein glycotransferase, Mv1749, MVO1749
ECTree
2.4.99.21 dolichyl-phosphooligosaccharide-protein glycotransferaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.4.99.21 - dolichyl-phosphooligosaccharide-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
an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine
an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyl)-N-acetyl-alpha-D-glucosaminyl phosphate + Ac-YKYQESSYK-(4-nitro)F-NH2
dolichol + ?
the peptide is based on the sequence of the natively glycosylated flagellum protein FlaB2. The enzyme shows no activity with the peptide Ac-YKYQESSYK-(4-nitro)F-NH2, lacking the key asparagine residue. Although the full length N-glycan generated by Methanococcus voltae (L-threonyl 2-(acetylamino)-2-deoxy-beta-D-mannuronamido-(1->4)-2,3-bis(acetylamino)-2,3-bis(acetylamino)-2,3-dideoxy-beta-D-glucuronosyl-(1->3)-2-(acetylamino)-2-deoxy-beta-D-glucosyl-[protein]-L-asparagine) is a trisaccharide the disaccharide-linked substrate is sufficient for oligosaccharyl transferase activity
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?
dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyl)-N-acetyl-alpha-D-glucosaminyl phosphate + [flagellum protein FlaB2]-L-asparagine
dolichol + 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyl)-N-acetyl-alpha-D-glucosaminyl-[flagellum protein FlaB2]-L-asparagine
the enzyme is incubated with the acceptor peptide Ac-YKYQESSYK-(4-nitro)F-NH2, which is based the natively glycosylated flagellum protein FlaB2 sequence. The activity is dependent on the canonical AsnXaaSer/Thr sequon. Although the full length N-glycan generated by Methanococcus voltae (L-threonyl 2-(acetylamino)-2-deoxy-beta-D-mannuronamido-(1->4)-2,3-bis(acetylamino)-2,3-bis(acetylamino)-2,3-dideoxy-beta-D-glucuronosyl-(1->3)-2-(acetylamino)-2-deoxy-beta-D-glucosyl-[protein]-L-asparagine) is a trisaccharide the disaccharide-linked substrate is sufficient for oligosaccharyl transferase activity
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-
?
dolichyl phosphooligosaccharide + [flagellum protein FlaB2]-L-asparagine101
dolichol + flagellum protein FlaB2 with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
the enzyme participates in the N-linked glycosylation in Methanococcus voltae. It catalyzes transfer of oligosaccharides from the dolichyl phosphate donor to asparagine in the acceptor proteins. The activity is dependent on the canonical AsnXaaSer/Thr sequon. Although the full length N-glycan generated by Methanococcus voltae (L-threonyl 2-(acetylamino)-2-deoxy-beta-D-mannuronamido-(1->4)-2,3-bis(acetylamino)-2,3-bis(acetylamino)-2,3-dideoxy-beta-D-glucuronosyl-(1->3)-2-(acetylamino)-2-deoxy-beta-D-glucosyl-[protein]-L-asparagine) is a trisaccharide, the disaccharide-linked substrate is sufficient for oligosaccharyl transferase activity
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?
dolichyl phosphosulfoheptasaccharide + [protein]-L-asparagine
dolichyl phosphate + a glycoprotein with the sulfoheptasaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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-
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?
lipid-linked oligosaccharide + [peptide]-L-asparagine
lipid + a glycopeptide with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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the glycan structure is estimated to be a branched heptasaccharide
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?
an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine
an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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the oligosaccharide chain that Archaeoglobus fulgidus AglB-L transfers to the Asn residues in proteins has the structure alpha-D-Glcp-(1-6)-alpha-[(1-3)-alpha-D-GlcP]-D-Manp-(1-3)-alpha-D-Galp-(1-2)-alpha-D-Manp-(1-3)-[(1-4)-beta-D-Glcp]-beta-D-Galp-(1-4)-beta-D-Glcp-Asn. The monosaccharide residue that is directly linked to the Asn residue is hexose
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?
an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine
an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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the Pyrococcus furiosus and Archaeoglobus fulgidus AglBs preferentially glycosylate sequons with Val and Glu at the X position, respectively
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?
an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine
an archaeal dolichyl phosphate + 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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?
an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine
an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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the Pyrococcus furiosus and Archaeoglobus fulgidus AglBs preferentially glycosylate sequons with Val and Glu at the X position, respectively
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?
additional information
?
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tethering an N-glycosylation sequon-containing peptide creates a catalytically competent oligosaccharyltransferase complex. The tethered peptide serves as an efficient substrate that receives the oligosaccharide chain from the lipid-linked oligosaccharide. The oligosaccharyl transfer is a single-turnover reaction, because it proceeds within the covalently cross-linked complex
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additional information
?
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tethering an N-glycosylation sequon-containing peptide creates a catalytically competent oligosaccharyltransferase complex. The tethered peptide serves as an efficient substrate that receives the oligosaccharide chain from the lipid-linked oligosaccharide. The oligosaccharyl transfer is a single-turnover reaction, because it proceeds within the covalently cross-linked complex
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additional information
?
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the enzyme (AglB) has the ability to attach incomplete glycans as seen by the disaccharides present on flagellins and S-layer proteins in Methanococcus voltae aglA mutant cells. AglA is the glycosyl transferase involved in the attachment of the terminal sugar to the glycan
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?
