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Literature summary extracted from

  • Miller, B.G.; Wolfenden, R.
    Catalytic proficiency: the unusual case of OMP decarboxylase (2002), Annu. Rev. Biochem., 71, 847-885.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.23 in complex with different ligands, e.g. 6-hydroxyuridine 5'-phosphate Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.23 D91A mutant with strongly reduced activity, incapable of binding substrate Saccharomyces cerevisiae
4.1.1.23 D96A active site mutant with increased dissociation constants for various ligands and strongly reduced activity Saccharomyces cerevisiae
4.1.1.23 K59A active site mutant with increased dissociation constants for various ligands and strongly reduced activity Saccharomyces cerevisiae
4.1.1.23 K93A mutant with strongly reduced activity, incapable of binding substrate Saccharomyces cerevisiae
4.1.1.23 R235A active site mutant with increased dissociation constants for various ligands Saccharomyces cerevisiae
4.1.1.23 Y217A active site mutant with increased dissociation constants for various ligands Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.23 5,6-dihydroorotidine 5'-phosphate
-
Saccharomyces cerevisiae
4.1.1.23 5-phosphoribofuranosylallopurinol
-
Saccharomyces cerevisiae
4.1.1.23 6-azauridine 5'-phosphate competitive inhibitor Saccharomyces cerevisiae
4.1.1.23 6-carboxyamidouridine 5'-phosphate
-
Saccharomyces cerevisiae
4.1.1.23 6-hydroxyuridine 5'-phosphate potent competitive inhibitor Saccharomyces cerevisiae
4.1.1.23 6-thiocarboxamidouridine 5'-phosphate
-
Saccharomyces cerevisiae
4.1.1.23 additional information not inhibited by 2-thioorotidine 5'-phosphate Saccharomyces cerevisiae
4.1.1.23 Orotate
-
Saccharomyces cerevisiae
4.1.1.23 phosphate
-
Saccharomyces cerevisiae
4.1.1.23 ribose 5-phosphate competitive inhibitor Saccharomyces cerevisiae
4.1.1.23 UMP
-
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 properties, catalytic proficiency/efficiency Saccharomyces cerevisiae
4.1.1.23 0.0007
-
orotidine 5'-phosphate
-
Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.23 additional information no metal ion requirement 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 Bacillus subtilis
-
UMP + CO2
-
?
4.1.1.23 Orotidine 5'-phosphate Escherichia coli
-
UMP + CO2
-
?
4.1.1.23 Orotidine 5'-phosphate Saccharomyces cerevisiae
-
UMP + CO2
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.23 Bacillus subtilis
-
-
-
4.1.1.23 Escherichia coli
-
-
-
4.1.1.23 Saccharomyces cerevisiae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.1.23 orotidine 5'-phosphate = UMP + CO2 mechanism Bacillus subtilis
4.1.1.23 orotidine 5'-phosphate = UMP + CO2 mechanism Escherichia coli
4.1.1.23 orotidine 5'-phosphate = UMP + CO2 mechanism Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.23 additional information 2-thioorotidine 5'-phosphate is 10000000fold less reactive than orotidine 5'-phosphate as substrate, not: 2-thiouridine 5'-phosphate Saccharomyces cerevisiae ?
-
?
4.1.1.23 Orotidine 5'-phosphate
-
Bacillus subtilis UMP + CO2
-
?
4.1.1.23 Orotidine 5'-phosphate
-
Escherichia coli UMP + CO2
-
?
4.1.1.23 Orotidine 5'-phosphate
-
Saccharomyces cerevisiae UMP + CO2
-
?
4.1.1.23 Orotidine 5'-phosphate catalytic proficiency, activity does not depend on the formation of a covalent bond to the substrate, catalyzes the reaction through noncovalent binding interactions that involve only the functional groups of its constituent amino acids, catalytic mechanism, mechanism of transition state stabilization, active site structure, role of Lys-93 Saccharomyces cerevisiae UMP + CO2
-
ir
4.1.1.23 Orotidine 5'-phosphate mechanism, enzyme structure Bacillus subtilis UMP + CO2
-
?
4.1.1.23 Orotidine 5'-phosphate mechanism, enzyme structure Escherichia coli UMP + CO2
-
?

Subunits

EC Number Subunits Comment Organism
4.1.1.23 homodimer active form, two independently operating active sites per dimer, located at the interface between subunits 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 additional information
-
additional information
-
Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.23 6.9
-
-
Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.23 additional information no cofactor requirement Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.1.1.23 0.0000000088
-
6-hydroxyuridine 5'-phosphate
-
Saccharomyces cerevisiae
4.1.1.23 0.000064
-
6-azauridine 5'-phosphate
-
Saccharomyces cerevisiae
4.1.1.23 0.08
-
ribose 5-phosphate
-
Saccharomyces cerevisiae
4.1.1.23 0.2
-
UMP
-
Saccharomyces cerevisiae