EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.4.99.21 | more |
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 |
Archaeoglobus fulgidus |
? |
- |
- |
2.4.99.21 | more |
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 |
Archaeoglobus fulgidus ATCC 49558 |
? |
- |
- |
2.4.99.21 | an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine |
- |
Haloferax volcanii |
an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine |
- |
? |
2.4.99.21 | an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine |
- |
Archaeoglobus fulgidus |
an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine |
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 |
? |
2.4.99.21 | an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine |
the Pyrococcus furiosus and Archaeoglobus fulgidus AglBs preferentially glycosylate sequons with Val and Glu at the X position, respectively |
Pyrococcus furiosus |
an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine |
- |
? |
2.4.99.21 | an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine |
the Pyrococcus furiosus and Archaeoglobus fulgidus AglBs preferentially glycosylate sequons with Val and Glu at the X position, respectively |
Archaeoglobus fulgidus |
an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine |
- |
? |
2.4.99.21 | dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyl)-N-acetyl-alpha-D-glucosaminyl phosphate + Ac-YKYQESSYK-(4-nitro)F-NH2 |
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 |
Methanococcus voltae |
dolichol + ? |
- |
? |
2.4.99.21 | dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyl)-N-acetyl-alpha-D-glucosaminyl phosphate + [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 |
Methanococcus voltae |
dolichol + 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyl)-N-acetyl-alpha-D-glucosaminyl-[flagellum protein FlaB2]-L-asparagine |
- |
? |
2.4.99.21 | dolichyl phosphooligosaccharide + [flagellum protein FlaB2]-L-asparagine101 |
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 |
Methanococcus voltae |
dolichol + flagellum protein FlaB2 with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine |
- |
? |
2.4.99.21 | dolichyl phosphosulfoheptasaccharide + [protein]-L-asparagine |
- |
Archaeoglobus fulgidus |
dolichyl phosphate + a glycoprotein with the sulfoheptasaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine |
- |
? |