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Literature summary for 4.1.1.23 extracted from

  • Langdon, S.D.; Jones, M.E.
    Study of the kinetic and physical properties of the orotidine-5'-monophosphate decarboxylase domain from mouse UMP synthase produced in Saccharomyces cerevisiae (1987), J. Biol. Chem., 262, 13359-13365.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of the orotidine-5'-phosphate decarboxylase domain of the bifunctional enzyme UMP synthase in Saccharomyces cerevisiae Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
6-azauridine 5'-phosphate
-
Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00026
-
orotidine 5'-phosphate orotidine-5'-phosphate decarboxylase domain of the bifunctional enzyme UMP synthase, 20°C Mus musculus
0.000615
-
orotidine 5'-phosphate orotidine-5'-phosphate decarboxylase domain of the bifunctional enzyme UMP synthase, 37°C Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
the orotidine-5'-phosphate decarboxylase domain of the bifunctional enzyme UMP synthase has a MW of 27814, calculation from amino acid sequence Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
bifunctional UMP synthase contains activities of EC 2.4.2.10 and EC 4.1.1.23
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Orotidine 5'-phosphate
-
Mus musculus UMP + CO2
-
?

Subunits

Subunits Comment Organism
More the orotidine-5'-phosphate decarboxylase domain of the bifunctional enzyme UMP synthase forms a dimer in the presence of ligands Mus musculus