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

BRENDA support

Literature summary extracted from

  • Spirig, U.; Bodmer, D.; Wacker, M.; Burda, P.; Aebi, M.
    The 3.4-kDa Ost4 protein is required for the assembly of two distinct oligosaccharyltransferase complexes in yeast (2005), Glycobiology, 15, 1396-1406.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.99.18 500000
-
 non-denaturing gel electrophoresis Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine Saccharomyces cerevisiae oligosaccharyltransferase complex catalyzes the transfer of a lipid-linked core oligosaccharide onto asparagine residues of nascent polypeptide chains in the lumen of the endoplasmic reticulum dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
 ?

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 + [protein]-N-oligosaccharidyl-L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine oligosaccharyltransferase complex catalyzes the transfer of a lipid-linked core oligosaccharide onto asparagine residues of nascent polypeptide chains in the lumen of the endoplasmic reticulum Saccharomyces cerevisiae dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.99.18 More six different subunits are detected in the wild-type complex, including Stt3p, Ost1p, Wbp1p, Swp1p, Ost3p, and Ost6p. The small 3.4-kDa subunit Ost4p is required for the incorporation of either Ost3p or Ost6p into the complex, resulting in two, functionally distinct OTase complexes in vivo. Ost3p and Ost6p are not absolutely required for OTase activity, but modulate the affinity of the enzyme toward different protein substrates Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
2.4.99.18 oligosaccharyltransferase
-
 Saccharomyces cerevisiae
2.4.99.18 OTase
-
 Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.99.18 7.5
-
 assay at Saccharomyces cerevisiae