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Literature summary 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.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.23
-
 Saccharomyces cerevisiae

General Stability

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.23 1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid high affinity inhibitor Saccharomyces cerevisiae
4.1.1.23 6-azauridine 5'-phosphate competitive inhibitor Saccharomyces cerevisiae
4.1.1.23 6-thiocarboxamidouridine 5'-phosphate
-
 Saccharomyces cerevisiae
4.1.1.23 8-azaxanthosine 5'-phosphate
-
 Saccharomyces cerevisiae
4.1.1.23 allopurinol beta-D-riboside 5'-phosphate
-
 Saccharomyces cerevisiae
4.1.1.23 oxypurinol 5'-phosphate
-
 Saccharomyces cerevisiae
4.1.1.23 ribose 5-phosphate
-
 Saccharomyces cerevisiae
4.1.1.23 thiopurinol 5'-phosphate
-
 Saccharomyces cerevisiae
4.1.1.23 UMP ineffective inhibitor Saccharomyces cerevisiae
4.1.1.23 xanthosine 5'-phosphate
-
 Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.23 additional information
-
 additional information kinetic data and mechanism Saccharomyces cerevisiae
4.1.1.23 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

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Reaction

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

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
-
 ?
4.1.1.23 Orotidine 5'-phosphate enzyme has two functionally independent substrate binding sites Saccharomyces cerevisiae UMP + CO2
-
 ?

Subunits

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.23 25
-
 assay at Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.23 14 20 orotidine 5'-phosphate pH 7.2, 25°C, not affected by NaCl concentration Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.23 7.2
-
 assay at Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.1.1.23 0.000052
-
 oxypurinol 5'-phosphate
-
 Saccharomyces cerevisiae
4.1.1.23 0.000093
-
 6-azauridine 5'-phosphate
-
 Saccharomyces cerevisiae
4.1.1.23 0.00012
-
 8-azaxanthosine 5'-phosphate
-
 Saccharomyces cerevisiae
4.1.1.23 0.0025
-
 thiopurinol 5'-phosphate
-
 Saccharomyces cerevisiae
4.1.1.23 0.004
-
 allopurinol beta-D-riboside 5'-phosphate
-
 Saccharomyces cerevisiae
4.1.1.23 0.024
-
 xanthosine 5'-phosphate
-
 Saccharomyces cerevisiae
4.1.1.23 0.2 0.4 UMP
-
 Saccharomyces cerevisiae
4.1.1.23 0.5
-
 ribose 5-phosphate
-
 Saccharomyces cerevisiae