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Literature summary for 4.1.1.23 extracted from

  • Floyd, E.E.; Jones, M.E.
    Isolation and characterization of the orotidine 5'-monophosphate decarboxylase domain of the multifunctional protein uridine 5'-monophosphate synthase (1985), J. Biol. Chem., 260, 9443-9451.
    View publication on PubMed

General Stability

General Stability Organism
glycerol, 50% v/v is an effective stabilizer of the orotidine-5'-phosphate decarboxylase domain at 4°C, -20°C or -70°C Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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bifunctional UMP synthase contains activities of EC 2.4.2.10 and EC 4.1.1.23
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Purification (Commentary)

Purification (Comment) Organism
preparation and isolation of the orotidine-5'-phosphate decarboxylase domain of UMP synthase Mus musculus

Storage Stability

Storage Stability Organism
-70°C, dilute buffer plus 2 mM dithiothreitol, purified UMP synthase activity retains orotidine-5'-phosphate decarboxylase activity for several months Mus musculus
0°C or -70°C, 5 mM potassium phosphate, pH 7.0, 2 mM dithiothreitol, rapid loss of orotidine-5'-phosphate decarboxylase activity of the orotidine-5'-phosphate decarboxylase domain of UMP synthase Mus musculus

Substrates and Products (Substrate)

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