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Literature summary extracted from

  • Vowels, J.J.; Payne, G.S.
    A role for the lumenal domain in Golgi localization of the Saccharomyces cerevisiae guanosine diphosphatase (1998), Mol. Biol. Cell, 9, 1351-1365.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.1.42 GDA1 gene Saccharomyces cerevisiae

General Stability

EC Number General Stability Organism
3.6.1.42 very stable Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.1.42 Golgi apparatus Golgi localization Saccharomyces cerevisiae 5794
-
3.6.1.42 Golgi apparatus distribution in multiple compartments Saccharomyces cerevisiae 5794
-
3.6.1.42 Golgi lumen large catalytic lumenal domain Saccharomyces cerevisiae 5796
-
3.6.1.42 membrane type II integral membrane glycoprotein with a short amino-terminal cytoplasmic domain, which is not sufficient for Golgi localization, a single transmembrane domain , and a large catalytic lumenal domain, which is required for activity Saccharomyces cerevisiae 16020
-
3.6.1.42 additional information subcellular localization Saccharomyces cerevisiae
-
-
3.6.1.42 additional information Golgi localization Saccharomyces cerevisiae
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.6.1.42 additional information
-
-
 Saccharomyces cerevisiae
3.6.1.42 55000
-
 after signal sequence cleavage, metabolic labeling and immunoprecipitation, SDS-PAGE Saccharomyces cerevisiae
3.6.1.42 57000
-
 before signal sequence cleavage, metabolic labeling and immunoprecipitation, SDS-PAGE Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.42 GDP + H2O Saccharomyces cerevisiae cleaves GDP that originates from GDP-mannose after mannosylation of glycoproteins in Golgi complex 5'-GMP + phosphate
-
 ?
3.6.1.42 additional information Saccharomyces cerevisiae GDPase plays an important role in mannosylation of proteins and lipids by regulating the amount of GDP-mannose available in Golgi lumen ?
-
 ?
3.6.1.42 additional information Saccharomyces cerevisiae necessary for Golgi-specific glycosylation reactions ?
-
 ?
3.6.1.42 additional information Saccharomyces cerevisiae GDPase has an important role in glycosylation reactions in Golgi lumen ?
-
 ?
3.6.1.42 additional information Saccharomyces cerevisiae role in mannosylation ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.42 Saccharomyces cerevisiae
-
 wild-type and mutants
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.6.1.42 glycoprotein three potential N-glycosylation sites Saccharomyces cerevisiae
3.6.1.42 glycoprotein N-linked oligosaccharides Saccharomyces cerevisiae
3.6.1.42 proteolytic modification
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.42 GDP + H2O
-
 Saccharomyces cerevisiae 5'-GMP + phosphate
-
 ?
3.6.1.42 GDP + H2O cleaves GDP that originates from GDP-mannose after mannosylation of glycoproteins in Golgi complex Saccharomyces cerevisiae 5'-GMP + phosphate
-
 ?
3.6.1.42 additional information GDPase plays an important role in mannosylation of proteins and lipids by regulating the amount of GDP-mannose available in Golgi lumen Saccharomyces cerevisiae ?
-
 ?
3.6.1.42 additional information necessary for Golgi-specific glycosylation reactions Saccharomyces cerevisiae ?
-
 ?
3.6.1.42 additional information GDPase has an important role in glycosylation reactions in Golgi lumen Saccharomyces cerevisiae ?
-
 ?
3.6.1.42 additional information role in mannosylation Saccharomyces cerevisiae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.6.1.42 More
-
 Saccharomyces cerevisiae