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Literature summary for 4.1.1.23 extracted from

  • Appleby, T.C.; Kinsland, C.; Begley, T.P.; Ealick, S.E.
    The crystal structure and mechanism of orotidine 5'-monophosphate decarboxylase (2000), Proc. Natl. Acad. Sci. USA, 97, 2005-2010.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.1.23

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(DE3) Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray crystal structure with bound uridine 5’-monophosphate Bacillus subtilis

General Stability

General Stability Organism
unliganded enzyme without bound UMP or OMP forms heavy precipitates during purification Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Orotidine 5'-phosphate Bacillus subtilis catalyzes the final step in the de novo biosynthesis of uridine monophosphate UMP + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P25971
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Bacillus subtilis

Reaction

Reaction Comment Organism Reaction ID
orotidine 5'-phosphate = UMP + CO2 reaction mechanism Bacillus subtilis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Orotidine 5'-phosphate catalytic mechanism, bimolecular electrophilic substitution mechanism in which decarboxylation and carbon-carbon bond protonation by Lys-62 occur in a concerted action, enzyme/active site structure, one active site per monomer, located near the dimer interface Bacillus subtilis UMP + CO2
-
 ?
Orotidine 5'-phosphate catalyzes the final step in the de novo biosynthesis of uridine monophosphate Bacillus subtilis UMP + CO2
-
 ?

Subunits

Subunits Comment Organism
homodimer active form, subunit structure Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
additional information no cofactor requirement Bacillus subtilis