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Literature summary for 2.4.99.18 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
Search for more literature for 2.4.99.18

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dolichyl diphosphooligosaccharide + N-benzoyl-Asn-Gly-D-allo-Thr-NHCH3
-
 Sus scrofa ?
-
 ?
dolichyl diphosphooligosaccharide + N-benzoyl-Asn-Gly-L-threo-beta-hydroxynorvaline-NHCH3
-
 Sus scrofa ?
-
 ?
dolichyl diphosphooligosaccharide + N-benzoyl-Asn-Gly-Ser-NHCH3
-
 Sus scrofa ?
-
 ?
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
-
 ?
dolichyl-diphosphochitobiose + N-benzoyl-Asn-Gly-Thr-NHCH3
-
 Sus scrofa ?
-
 ?
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 ?
-
 ?