Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.99.18 extracted from

  • Jamaluddin, M.F.; Bailey, U.M.; Tan, N.Y.; Stark, A.P.; Schulz, B.L.
    Polypeptide binding specificities of Saccharomyces cerevisiae oligosaccharyltransferase accessory proteins Ost3p and Ost6p (2011), Protein Sci., 20, 849-855.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.99.18

Protein Variants

Protein Variants Comment Organism
Q103K/Q106K introducing basic residues in place of the wild-type neutral residues lining the peptide-binding groove of Ost3p, allows binding of a hydrophobic and acidic peptide. MBP-Ost3Q103K,Q106K variant shows significant binding to the peptide Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum membrane reaction takes place in the lumen Saccharomyces cerevisiae 5789
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dolichyl diphosphooligosaccharide + [protein]-L-asparagine Saccharomyces cerevisiae
-
 dolichyl diphosphate + [protein]-L-asparagine-N-oligosaccharide a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P48439 isozyme Ost3p
-
Saccharomyces cerevisiae Q03723 isozyme Ost6p
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dolichyl diphosphooligosaccharide + [protein]-L-asparagine
-
 Saccharomyces cerevisiae dolichyl diphosphate + [protein]-L-asparagine-N-oligosaccharide a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine ?

Synonyms

Synonyms Comment Organism
oligosaccharyltransferase
-
 Saccharomyces cerevisiae
Ost3p
-
 Saccharomyces cerevisiae
Ost6p
-
 Saccharomyces cerevisiae
OTase
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
additional information Ost3p structure-function relationship, overview Saccharomyces cerevisiae
additional information Ost6p structure-function relationship, overview Saccharomyces cerevisiae
physiological function asparagine-linked glycosylation is a common and vital co- and post-translocational modification of diverse secretory and membrane proteins in eukaryotes that is catalyzed by the multiprotein complex oligosaccharyltransferase. Isozymes Ost3p or Ost6p possess different protein substrate specificities at the level of individual glycosylation sites, model of Ost3/6p function in which they transiently bind stretches of nascent polypeptide substrate to inhibit protein folding, thereby increasing glycosylation efficiency at nearby asparagine residues Saccharomyces cerevisiae
physiological function asparagine-linked glycosylation is a common and vital co- and post-translocational modification of diverse secretory and membrane proteins in eukaryotes that is catalyzed by the multiprotein complex oligosaccharyltransferase. Ispzymes Ost3p or Ost6p possess different protein substrate specificities at the level of individual glycosylation sites. Ost6p, which has a peptide-binding groove with a strongly hydrophobic base lined by neutral and basic residues, binds peptides enriched in hydrophobic and acidic amino acids. Model of Ost3/6p function in which they transiently bind stretches of nascent polypeptide substrate to inhibit protein folding, thereby increasing glycosylation efficiency at nearby asparagine residues Saccharomyces cerevisiae