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Literature summary for 4.1.1.23 extracted from

  • Wise, E.; Yew, W.S.; Babbitt, P.C.; Gerlt, J.A.; Rayment, I.
    Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase (2002), Biochemistry, 41, 3861-3869.
    View publication on PubMed
Search for more literature for 4.1.1.23

Metals/Ions

Metals/Ions Comment Organism Structure
additional information metal-independent reaction Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Orotidine 5'-phosphate Bacillus subtilis
-
 UMP + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Orotidine 5'-phosphate
-
 Bacillus subtilis UMP + CO2
-
 ?
Orotidine 5'-phosphate mechansim, no formation of a vinyl anion intermediate, enzyme structure, the active sites are located at the dimer interface Bacillus subtilis UMP + CO2
-
 ?

Subunits

Subunits Comment Organism
dimer each subunit consists of a (beta/alpha)8-barrel, arranged in an antiparallel manner Bacillus subtilis

Synonyms

Synonyms Comment Organism
OMPDC
-
 Bacillus subtilis