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Literature summary for 2.4.99.18 extracted from

  • Pathak, R.; Imperiali, B.
    A dual affinity tag on the 64-kDa Nlt1p subunit allows the rapid characterization of mutant yeast oligosaccharyl transferase complexes (1997), Arch. Biochem. Biophys., 338, 1-6.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
creation of a yeast strain in which the essential 64000 Da glycoprotein Nlt1p subunit of the oligosaccharyl transferase is modified by the addition of a 22-residue carboxy-terminal affinity tag, the tag includes both an 8-residue FLAG epitope and a 6-residue histidine motif Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Saccharomyces cerevisiae 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
lipid-linked oligosaccharide + unfolded nascent polypeptide chain Saccharomyces cerevisiae the enzyme catalyzes the glycosylation of selected asparagine residues of nascent polypeptide chains as they are translocated into the lumen of the endoplasmic reticulum ?
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
purification of an affinity-tagged version of the enzyme complex from a membrane protein fraction Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dolichyl diphosphooligosaccharide + protein L-asparagine
-
Saccharomyces cerevisiae dolichyl diphosphate + glycoprotein with the oligosaccharide chain attached by N-glycosyl-linkage to protein L-asparagine
-
?
lipid-linked oligosaccharide + unfolded nascent polypeptide chain the enzyme catalyzes the glycosylation of selected asparagine residues of nascent polypeptide chains as they are translocated into the lumen of the endoplasmic reticulum Saccharomyces cerevisiae ?
-
?

Subunits

Subunits Comment Organism
More heteromeric complex of five subunits Saccharomyces cerevisiae