Literature summary for 4.1.1.23 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.

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KM Value [mM]

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	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	-	Homo sapiens	UMP + CO2	-	?

Temperature Stability [°C]

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

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Release 2023.1 (January 2023)