Literature summary for 4.1.1.23 extracted from

Porter, D.J.T.; Short, S.A.
Yeast orotidine-5'-phosphate decarboxylase: steady-state and pre-steady-state analysis of the kinetic mechanism of substrate decarboxylation (2000), Biochemistry, 39, 11788-11800.

Search for more literature for 4.1.1.23

Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Saccharomyces cerevisiae

General Stability

General Stability	Organism
NaCl stabilizes the dimeric active enzyme form	Saccharomyces cerevisiae

Inhibitors

Inhibitors	Comment	Organism	Structure
1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid	high affinity inhibitor	Saccharomyces cerevisiae
6-azauridine 5'-phosphate	competitive inhibitor	Saccharomyces cerevisiae
6-thiocarboxamidouridine 5'-phosphate	-	Saccharomyces cerevisiae
8-azaxanthosine 5'-phosphate	-	Saccharomyces cerevisiae
allopurinol beta-D-riboside 5'-phosphate	-	Saccharomyces cerevisiae
oxypurinol 5'-phosphate	-	Saccharomyces cerevisiae
ribose 5-phosphate	-	Saccharomyces cerevisiae
thiopurinol 5'-phosphate	-	Saccharomyces cerevisiae
UMP	ineffective inhibitor	Saccharomyces cerevisiae
xanthosine 5'-phosphate	-	Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetic data and mechanism	Saccharomyces cerevisiae
0.001	0.002	orotidine 5'-phosphate	Km value is very dependent on the NaCl concentration, NaCl increases the Km value	Saccharomyces cerevisiae

Metals/Ions

Metals/Ions	Comment	Organism	Structure
additional information	no metal cofactor	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
Orotidine 5'-phosphate	Saccharomyces cerevisiae	-	UMP + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
orotidine 5'-phosphate = UMP + CO2	kinetic mechanism	Saccharomyces cerevisiae	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Orotidine 5'-phosphate	-	Saccharomyces cerevisiae	UMP + CO2	-	?
Orotidine 5'-phosphate	enzyme has two functionally independent substrate binding sites	Saccharomyces cerevisiae	UMP + CO2	-	?

Subunits

Subunits	Comment	Organism
dimer	catalytically active form, substrate-induced enzyme dimerization	Saccharomyces cerevisiae

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
14	20	orotidine 5'-phosphate	pH 7.2, 25°C, not affected by NaCl concentration	Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.2	-	assay at	Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.000052	-	oxypurinol 5'-phosphate	-	Saccharomyces cerevisiae
0.000093	-	6-azauridine 5'-phosphate	-	Saccharomyces cerevisiae
0.00012	-	8-azaxanthosine 5'-phosphate	-	Saccharomyces cerevisiae
0.0025	-	thiopurinol 5'-phosphate	-	Saccharomyces cerevisiae
0.004	-	allopurinol beta-D-riboside 5'-phosphate	-	Saccharomyces cerevisiae
0.024	-	xanthosine 5'-phosphate	-	Saccharomyces cerevisiae
0.2	0.4	UMP	-	Saccharomyces cerevisiae
0.5	-	ribose 5-phosphate	-	Saccharomyces cerevisiae

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)