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

BRENDA support

Literature summary extracted from

  • Janik, A.; Sosnowska, M.; Kruszewska, J.; Krotkiewski, H.; Lehle, L.; Palamarczyk, G.
    Overexpression of GDP-mannose pyrophosphorylase in Saccharomyces cerevisiae corrects defects in dolichol-linked saccharide formation and protein glycosylation (2003), Biochim. Biophys. Acta, 1621, 22-30.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.13 0.78
-
GDPmannose pH 7.8, 37°C Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.83 additional information Saccharomyces cerevisiae increased availability of GDP-mannose corrects glycosylation defects in the endoplasmic reticulum, such as dolichyl D-mannosyl phosphate formation in dolichyl-phosphate beta-D-mannosyltransferase mutants of Saccharomyces cerevisiae ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.83 Saccharomyces cerevisiae
-
-
-
2.7.7.13 Saccharomyces cerevisiae P41940 Saccharomyces cerevisiae genome database: U24437; overexpression corrects defects in dolichol-linked saccharide formation and protein glycosylation
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.83 additional information increased availability of GDP-mannose corrects glycosylation defects in the endoplasmic reticulum, such as dolichyl D-mannosyl phosphate formation in dolichyl-phosphate beta-D-mannosyltransferase mutants of Saccharomyces cerevisiae Saccharomyces cerevisiae ?
-
?
2.7.7.13 GTP + alpha-D-mannose 1-phosphate
-
Saccharomyces cerevisiae GDPmannose + diphosphate
-
?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.83 Dol-P-Man synthase
-
Saccharomyces cerevisiae