Literature summary extracted from

Fyfe, J.A.; Miller, R.L.; Krenitsky, T.A.
Kinetic properties and inhibition of orotidine 5'-phosphate decarboxylase. Effects of some allopurinol metabolites on the enzyme (1973), J. Biol. Chem., 248, 3801-3809.

General Stability

EC Number	General Stability	Organism
4.1.1.23	1-ribosyloxipurinol 5'-phosphate prevents loss of activity during preincubation in absence of substrate, when the inhibitor concentration is high enough to inhibit the enzyme substantially	Saccharomyces cerevisiae

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
4.1.1.23	1-Ribosyloxipurinol 5'-phosphate	most effective oxipurinol nucleotide inhibitor	Saccharomyces cerevisiae
4.1.1.23	3-Xanthosine 5'-phosphate	-	Saccharomyces cerevisiae
4.1.1.23	7-Ribosyloxipurinol 5'-phosphate	-	Saccharomyces cerevisiae
4.1.1.23	oxipurinol nucleotides	potent, competitive, bimodal. The inhibition of the enzyme by oxipurinol nucleotides is primarily responsible for the increased urinary excretion of orotic acid and orotidine in patients treated with allopurinol	Saccharomyces cerevisiae

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.1.1.23	Saccharomyces cerevisiae	-	-	-

Substrates and Products (Substrate)

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

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
4.1.1.23	25	-	half life: 26 min	Saccharomyces cerevisiae
4.1.1.23	37	-	half-life: 10 min. Nucleotide inhibitors stabilize against inactivation at 37°C	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)