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Literature summary extracted from

  • Haselbeck, A.
    Purification of GDP mannose:dolichyl-phosphate O-beta-D-mannosyltransferase from Saccharomyces cerevisiae (1989), Eur. J. Biochem., 181, 663-668.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.83 endoplasmic reticulum lumen Saccharomyces cerevisiae 5783
-
2.4.1.83 membrane enzyme is anchored with both its N-termini and C-termini in the membrane, while the main part of the protein is oriented towards the lumen of the endoplasmic reticulum Saccharomyces cerevisiae 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.83 30000
-
 x * 30000, SDS-PAGE Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.83 Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.4.1.83 additional information no glycosylation Saccharomyces cerevisiae

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.83
-
 Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.83 0.475
-
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.83 GDPmannose + dolichyl phosphate
-
 Saccharomyces cerevisiae GDP + dolichyl D-mannosyl phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.83 ? x * 30000, SDS-PAGE Saccharomyces cerevisiae