Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.1.23 extracted from

  • Harris, P.; Poulsen, J.C.N.; Jensen, K.F.; Larsen, S.
    Substrate binding induces domain movements in orotidine 5'-monophosphate decarboxylase (2002), J. Mol. Biol., 318, 1019-1029.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
uncomplexed apoenzyme and complexed with 1-(5’-phospho-beta-D-ribofuranosyl)barbituric acid Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no metals Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Orotidine 5'-phosphate enzyme/active site structure, contains two independently functioning active sites, binding of the phosphoryl group of the substrate is essential for the catalytic function, induced fit mechanism Escherichia coli UMP + CO2
-
?
Orotidine 5'-phosphate last step in the de novo synthesis of pyrimidine nucleotides Escherichia coli UMP + CO2
-
?

Subunits

Subunits Comment Organism
homodimer
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
additional information no cofactors Escherichia coli