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Literature summary extracted from

  • Karaoglu, D.; Kelleher, D.J.; Gilmore, R.
    Allosteric regulation provides a molecular mechanism for preferential utilization of the fully assembled dolichol-linked oligosaccharide by the yeast oligosaccharyltransferase (2001), Biochemistry, 40, 12193-12206.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.99.18 0.00015
-
 Nalpha-Ac-Asn-Tyr-Thr-NH2
-
 Saccharomyces cerevisiae
2.4.99.18 0.021
-
 dolichyl-diphosphochitobiose-(Man)9-(Glc)3
-
 Saccharomyces cerevisiae
2.4.99.18 0.0315
-
 dolichyl-diphosphochitobiose-(Man)9
-
 Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
2.4.99.18 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.99.18 dolichyl diphosphooligosaccharide + protein L-asparagine
-
 Saccharomyces cerevisiae dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
-
 ?
2.4.99.18 dolichyl-diphosphochitobiose-Man9 + Nalpha-Ac-Asn-Tyr-Thr-NH2
-
 Saccharomyces cerevisiae ?
-
 ?
2.4.99.18 dolichyl-diphosphochitobiose-Man9Glc3 + alpha-Ac-Asn-Tyr-Thr-NH2
-
 Saccharomyces cerevisiae ?
-
 ?
2.4.99.18 additional information allosteric communication between regulatory and catalytic dolichol-linked oligosaccharide binding sites Saccharomyces cerevisiae ?
-
 ?