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Literature summary for 4.1.1.23 extracted from

  • Harris, P.; Poulsen, J.C.N.; Jensen, K.F.; Larsen, S.
    Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase (2000), Biochemistry, 39, 4217-4224.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli NF 1830, expression of selenomethionine-substituted ODCase in Escherichia coli SO 6733 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
complexed with the inhibitor 1-(5’-phospho-beta-D-ribofuranosyl)barbituric acid Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid mode of binding Escherichia coli
UMP weak inhibitor Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.001
-
orotidine 5'-phosphate pH 7, increases to either side of pH 7 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no metal ion requirement Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Orotidine 5'-phosphate Escherichia coli catalyzes the last step in the de novo synthesis of UMP UMP + CO2
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
orotidine 5'-phosphate = UMP + CO2 catalytic mechanism Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
same specific activity of native and selenomethionine-substituted ODCase Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-Thioorotidine 5'-phosphate partially active substrate Escherichia coli 4-Thiouridine 5'-phosphate + CO2
-
?
Orotidine 5'-phosphate catalytic mechanism, role of Lys-93 in catalysis, enzyme structure Escherichia coli UMP + CO2
-
?
Orotidine 5'-phosphate catalyzes the last step in the de novo synthesis of UMP Escherichia coli UMP + CO2
-
?

Subunits

Subunits Comment Organism
homodimer dimer is composed of two alpha/beta-barrels with two shared active sites Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information very proficient enzyme Escherichia coli
2 8 orotidine 5'-phosphate pH 7, constant above pH 7, declines below pH 7 Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
very sharp Escherichia coli

Cofactor

Cofactor Comment Organism Structure
additional information no cofactor requirement Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00001
-
1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid below Escherichia coli
0.5
-
UMP
-
Escherichia coli