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Literature summary extracted from

  • Welply, J.K.; Shenbagamurthi, P.; Lennarz, W.J.; Naider, F.
    Substrate recognition by oligosaccharyltransferase. Studies on glycosylation of modified Asn-X-Thr/Ser tripeptides (1983), J. Biol. Chem., 258, 11856-11863.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.99.18 Ca2+
-
 Gallus gallus
2.4.99.18 Cu2+
-
 Gallus gallus
2.4.99.18 EDTA
-
 Gallus gallus
2.4.99.18 Mg2+ no inhibition Gallus gallus
2.4.99.18 N-benzoyl-Asn-Leu-Thr
-
 Gallus gallus
2.4.99.18 N-octanoyl-Asn-Leu-Thr
-
 Gallus gallus
2.4.99.18 N-t-butoxycarbonyl-Asn-Leu-Thr
-
 Gallus gallus
2.4.99.18 Zn2+
-
 Gallus gallus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.99.18 additional information
-
 additional information kinetic study with intact microsomal membrane. Km-value for Nalpha-Ac-Asn-Leu-Thr-NHCH3 is 0.01 mM Gallus gallus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.99.18 microsome luminal face of membrane Gallus gallus
-
-
2.4.99.18 rough endoplasmic reticulum the enzyme is oriented at the luminal face of the endoplasmic membrane Gallus gallus 5791
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.99.18 Mn2+ requirement Gallus gallus

Organism

EC Number Organism UniProt Comment Textmining
2.4.99.18 Gallus gallus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.99.18 oviduct
-
 Gallus gallus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.99.18 dolichyl diphosphooligosaccharide + 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 Gallus gallus dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + protein L-asparagine Asn-Xaa-Thr/Ser is a necessary and sufficient prerequisite for N-glycosylation Gallus gallus dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + protein L-asparagine peptide acceptor specificity Gallus gallus dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + synthetic tripeptides no substrates are Asn-Leu-Thr-derivatives containing asparagine modifications or substitution Gallus gallus ?
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + synthetic tripeptides peptide hydrophobicity increases its acceptor activity Gallus gallus ?
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + synthetic tripeptides Asn-Leu-Thr and its N-terminal acetyl-, benzoyl-, octanoyl- or t-butoxycarbonyl-derivatives Gallus gallus ?
-
 ?