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Literature summary for 4.1.1.23 extracted from

  • Wu, N.; Mo, Y.; Gao, J.; Pai, E.F.
    Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase (2000), Proc. Natl. Acad. Sci. USA, 97, 2017-2022.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Methanothermobacter thermautotrophicus

Crystallization (Commentary)

Crystallization (Comment) Organism
ligand-free ODCase form and complexed with 6-azauridine 5’-phosphate Methanothermobacter thermautotrophicus

Inhibitors

Inhibitors Comment Organism Structure
6-azauridine 5'-phosphate mode of binding Methanothermobacter thermautotrophicus
UMP weak inhibition Methanothermobacter thermautotrophicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Orotidine 5'-phosphate Methanothermobacter thermautotrophicus last step in the biosynthesis of pyrimidine nucleotides UMP + CO2
-
?

Organism

Organism UniProt Comment Textmining
Methanothermobacter thermautotrophicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Methanothermobacter thermautotrophicus

Reaction

Reaction Comment Organism Reaction ID
orotidine 5'-phosphate = UMP + CO2 catalytic mechanism Methanothermobacter thermautotrophicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Orotidine 5'-phosphate catalytic mechanism, the remarkable catalytic power is almost exclusively achieved via ground state destabilization of the reactive part of substrate, which is compensated for by strong binding of the phosphate and ribose groups, and to a lesser extend via transition state stabilization, enzyme/active site structure, mode of substrate binding Methanothermobacter thermautotrophicus UMP + CO2
-
?
Orotidine 5'-phosphate last step in the biosynthesis of pyrimidine nucleotides Methanothermobacter thermautotrophicus UMP + CO2
-
?

Subunits

Subunits Comment Organism
dimer
-
Methanothermobacter thermautotrophicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information remarkable catalytic power Methanothermobacter thermautotrophicus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.46
-
UMP
-
Methanothermobacter thermautotrophicus