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Literature summary extracted from

  • 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 (2001), FEBS Lett., 501, 106-110.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.99.18 0.16
-
 N-benzoyl-Asn-Gly-Thr-NHCH3
-
 Sus scrofa
2.4.99.18 0.6
-
 N-benzoyl-Asn-Gly-Ser-NHCH3
-
 Sus scrofa
2.4.99.18 4.3
-
 N-benzoyl-Asn-Gly-L-threo-beta-hydroxynorvaline-NHCH3
-
 Sus scrofa
2.4.99.18 12.5
-
 N-benzoyl-Asn-Gly-D-allo-Thr-NHCH3
-
 Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.99.18 lipid-linked oligosaccharide + unfolded nascent polypeptide chain Sus scrofa 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 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.99.18 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.99.18 liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.99.18 dolichyl diphosphooligosaccharide + N-benzoyl-Asn-Gly-D-allo-Thr-NHCH3
-
 Sus scrofa ?
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + N-benzoyl-Asn-Gly-L-threo-beta-hydroxynorvaline-NHCH3
-
 Sus scrofa ?
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + N-benzoyl-Asn-Gly-Ser-NHCH3
-
 Sus scrofa ?
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + 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 Sus scrofa dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
-
 ?
2.4.99.18 dolichyl-diphosphochitobiose + N-benzoyl-Asn-Gly-Thr-NHCH3
-
 Sus scrofa ?
-
 ?
2.4.99.18 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 Sus scrofa ?
-
 ?