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Literature summary for 4.1.1.2 extracted from

  • Reinhardt, L.A.; Svedruzic, D.; Chang, C.H.; Cleland, W.W.; Richards, N.G.J.
    Heavy atom isotope effects on the reaction catalyzed by the oxalate decarboxylase from Bacillus subtilis (2003), J. Am. Chem. Soc., 125, 1244-1252.
    View publication on PubMed
Search for more literature for 4.1.1.2

Activating Compound

Activating Compound Comment Organism Structure
O2 requires catalytic dioxygen for activity Bacillus subtilis

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic data, kinetic mechanism Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ contains Mn2+ in its resting state and two Mn-binding sites, may be only the C-terminal binding site is catalytically active, the N-terminal site not, manganese in the active site can abstract an electron from bound substrate Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
oxalate + H+ Bacillus subtilis
-
 formate + CO2
-
 ?
oxalate + H+ Bacillus subtilis 168
-
 formate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis 168
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant OXDC Bacillus subtilis

Reaction

Reaction Comment Organism Reaction ID
oxalate = formate + CO2 detailed catalytic mechanism, kinetic mechanism Bacillus subtilis
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxalate + H+
-
 Bacillus subtilis formate + CO2
-
 ?
oxalate + H+ mechanism, multistep model in which a reversible, proton-coupled, electron transfer from bound oxalate to the Mn-enzyme gives an oxalate radical, which decarboxylates to yield a formate radical anion, subsequent reduction and protonation of this intermediate then gives formate, irreversible decarboxylation step, no net redox change between substrate and products, roles of Arg-270 and Glu-333 in catalysis Bacillus subtilis formate + CO2
-
 ?
oxalate + H+
-
 Bacillus subtilis 168 formate + CO2
-
 ?
oxalate + H+ mechanism, multistep model in which a reversible, proton-coupled, electron transfer from bound oxalate to the Mn-enzyme gives an oxalate radical, which decarboxylates to yield a formate radical anion, subsequent reduction and protonation of this intermediate then gives formate, irreversible decarboxylation step, no net redox change between substrate and products, roles of Arg-270 and Glu-333 in catalysis Bacillus subtilis 168 formate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
More member of the cupin superfamily Bacillus subtilis
OXDC
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
21 22 assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
 pH-dependence of OxDC activity Bacillus subtilis