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Literature summary extracted from

  • Yablonski, M.J.; Pasek, D.A.; Han, B.D.; Jones, M.E.; Traut, T.W.
    Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylase (1996), J. Biol. Chem., 271, 10704-10708.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.4.2.10 additional information mutational separation of catalytic activity of enzyme and EC4.1.1.23 activity results in active but unstable proteins Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.23 0.000295
-
 orotidine 5'-phosphate orotidine-5'-phosphate decarboxylase domain of the bifunctional enzyme UMP synthase Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.10 Homo sapiens
-
-
-
4.1.1.23 Homo sapiens
-
 bifunctional UMP synthase contains activities of EC 2.4.2.10 and EC 4.1.1.23
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.23 Orotidine 5'-phosphate
-
 Homo sapiens UMP + CO2
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.1.23 25
-
 orotidine-5'-phosphate decarboxylase activity of UMP synthase, at low protein concentrations remains constant for 40 min Homo sapiens