Literature summary for 2.4.2.10 extracted from

Victor, J.; Greenberg, L.B.; Sloan, D.L.
Studies of the kinetic mechanism of orotate phosphoribosyltransferase from yeast (1979), J. Biol. Chem., 254, 2647-2655.

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Inhibitors

Inhibitors	Comment	Organism	Structure
5-phospho-alpha-D-ribose 1-diphosphate	phosphorolysis, product inhibition, kinetics	Saccharomyces cerevisiae
anthranilate	weak	Saccharomyces cerevisiae
arabinose 5-phosphate	at higher concentrations	Saccharomyces cerevisiae
diphosphate	product inhibition, kinetics	Saccharomyces cerevisiae
erythrose 4-phosphate	at higher concentrations	Saccharomyces cerevisiae
fructose 1-phosphate	at higher concentrations	Saccharomyces cerevisiae
fructose 6-phosphate	at higher concentrations	Saccharomyces cerevisiae
nicotinate	weak	Saccharomyces cerevisiae
Orotate	phosphorolysis, product inhibition, kinetics	Saccharomyces cerevisiae
orotidylate	product inhibition, kinetics	Saccharomyces cerevisiae
phosphate	at higher concentrations	Saccharomyces cerevisiae
ribose 5-phosphate	at higher concentrations	Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetic study	Saccharomyces cerevisiae
0.008	0.0083	orotidine 5'-phosphate	phosphorolysis	Saccharomyces cerevisiae
0.027	0.0275	Orotate	-	Saccharomyces cerevisiae
0.03	0.035	Orotate	-	Saccharomyces cerevisiae
0.038	0.04	5-phospho-alpha-D-ribose 1-diphosphate	-	Saccharomyces cerevisiae
0.096	-	diphosphate	phosphorolysis	Saccharomyces cerevisiae

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	requirement	Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
20000	-	2 * 20000, SDS-PAGE	Saccharomyces cerevisiae
40000	-	gel filtration	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	Budweiser brand	-

Reaction

Reaction	Comment	Organism	Reaction ID
orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate	mechanism is bi bi ping pong	Saccharomyces cerevisiae	a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
45	-	in the absence of added OMP-decarboxylase, EC 4.1.1.23	Saccharomyces cerevisiae
65	-	in the presence of added OMP-decarboxylase, EC 4.1.1.23	Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5-fluoroorotate + phosphoribose diphosphate	-	Saccharomyces cerevisiae	5-fluoroorotidine 5'-phosphate + diphosphate	-	?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate	catalyzes stereospecific formation of beta-glycosidic bond between orotate and ribose 5'-phosphate portion of phospho-ribose diphosphate	Saccharomyces cerevisiae	orotidine 5'-phosphate + diphosphate	-	r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate	predominant species of phosphoribose diphosphate: metal ion complex	Saccharomyces cerevisiae	orotidine 5'-phosphate + diphosphate	-	r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate	high specificity for orotate	Saccharomyces cerevisiae	orotidine 5'-phosphate + diphosphate	-	r

Subunits

Subunits	Comment	Organism
dimer	2 * 20000, SDS-PAGE	Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.01	-	orotydilate	-	Saccharomyces cerevisiae
0.042	-	5-phospho-alpha-D-ribose 1-diphosphate	-	Saccharomyces cerevisiae
0.063	-	Orotate	-	Saccharomyces cerevisiae
0.131	-	diphosphate	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)