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Literature summary extracted from

  • Tanner, A.; Bowater, L.; Fairhurst, S.A.; Bornemann, S.
    Oxalate decarboxylase requires manganese and dioxygen for activity. Overexpression and characterization of Bacillus subtilis YvrK and YoaN (2001), J. Biol. Chem., 276, 43627-43634.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.1.2 additional information induced by acidic pH and not by oxalate Bacillus subtilis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.2 yoaN gene, overexpression in Escherichia coli BL21(DE3)pLysS Bacillus subtilis
4.1.1.2 yvrK gene, overexpression in Escherichia coli BL21(DE3)pLysS Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.2 Dithionite 1 mM, complete loss of activity, some irreversible effect Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.2 15
-
 oxalate pH 5, 26°C, recombinant YvrK Bacillus subtilis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.1.1.2 soluble recombinant YoaN Bacillus subtilis
-
-
4.1.1.2 soluble recombinant YvrK Bacillus subtilis
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.2 Mn2+ specific requirement Bacillus subtilis
4.1.1.2 Mn2+ specific requirement for the correct folding and activity, contains between 0.86 and 1.14 atoms of manganese per subunit, predominantly in the Mn2+ oxidation state, both Mn2+ and O2 are cofactors acting together as a two-electron sink during catalysis Bacillus subtilis
4.1.1.2 additional information not: Fe2+, Cu2+, Ni2+, Co2+, Mg2+, Zn2+ Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.2 44000
-
 6 * 44000, recombinant YvrK, SDS-PAGE Bacillus subtilis
4.1.1.2 222000
-
 recombinant YvrK, nondenaturing PAGE Bacillus subtilis
4.1.1.2 254000
-
 recombinant YvrK, gel filtration Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.2 oxalate + H+ Bacillus subtilis oxalate-degrading enzyme formate + CO2
-
 ?
4.1.1.2 oxalate + H+ Bacillus subtilis oxalate-degrading enzyme, may be involved in the elevation of cytoplasmic pH, because the reaction involves the net consumption of a proton formate + CO2
-
 ?
4.1.1.2 oxalate + H+ Bacillus subtilis 168 oxalate-degrading enzyme formate + CO2
-
 ?
4.1.1.2 oxalate + H+ Bacillus subtilis 168 oxalate-degrading enzyme, may be involved in the elevation of cytoplasmic pH, because the reaction involves the net consumption of a proton formate + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.2 Bacillus subtilis O34714
-
-
4.1.1.2 Bacillus subtilis O34767
-
-
4.1.1.2 Bacillus subtilis 168 O34714
-
-
4.1.1.2 Bacillus subtilis 168 O34767
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
4.1.1.2 YvrK is occasionally prone to oxidation during the latter stages of the purification resulting in its dimerization, which is prevented by dithiothreitol Bacillus subtilis

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.2 recombinant YvrK, 20.7fold Bacillus subtilis

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.1.2 oxalate = formate + CO2 mechanism Bacillus subtilis
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.2 65
-
 pH 5, 26°C, recombinant YvrK Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.2 additional information enzyme catalyzes minor side reactions: oxalate oxidation to produce H2O2 and oxalate-dependent, H2O2-independent dye oxidations Bacillus subtilis ?
-
 ?
4.1.1.2 additional information enzyme catalyzes minor side reactions: oxalate oxidation to produce H2O2 and oxalate-dependent, H2O2-independent dye oxidations, at less than 1% of the oxalate decarboxylation rate Bacillus subtilis ?
-
 ?
4.1.1.2 additional information enzyme catalyzes minor side reactions: oxalate oxidation to produce H2O2 and oxalate-dependent, H2O2-independent dye oxidations Bacillus subtilis 168 ?
-
 ?
4.1.1.2 additional information enzyme catalyzes minor side reactions: oxalate oxidation to produce H2O2 and oxalate-dependent, H2O2-independent dye oxidations, at less than 1% of the oxalate decarboxylation rate Bacillus subtilis 168 ?
-
 ?
4.1.1.2 oxalate + H+ contains two potential active sites per subunit Bacillus subtilis formate + CO2
-
 ?
4.1.1.2 oxalate + H+ enzyme structure, YvrK possesses two potential active sites per subunit, but only one could be fully occupied by manganese, mechanism, catalytic cycle Bacillus subtilis formate + CO2
-
 ?
4.1.1.2 oxalate + H+ oxalate-degrading enzyme Bacillus subtilis formate + CO2
-
 ?
4.1.1.2 oxalate + H+ oxalate-degrading enzyme, may be involved in the elevation of cytoplasmic pH, because the reaction involves the net consumption of a proton Bacillus subtilis formate + CO2
-
 ?
4.1.1.2 oxalate + H+ contains two potential active sites per subunit Bacillus subtilis 168 formate + CO2
-
 ?
4.1.1.2 oxalate + H+ enzyme structure, YvrK possesses two potential active sites per subunit, but only one could be fully occupied by manganese, mechanism, catalytic cycle Bacillus subtilis 168 formate + CO2
-
 ?
4.1.1.2 oxalate + H+ oxalate-degrading enzyme Bacillus subtilis 168 formate + CO2
-
 ?
4.1.1.2 oxalate + H+ oxalate-degrading enzyme, may be involved in the elevation of cytoplasmic pH, because the reaction involves the net consumption of a proton Bacillus subtilis 168 formate + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.2 hexamer
-
 Bacillus subtilis
4.1.1.2 hexamer 6 * 44000, recombinant YvrK, SDS-PAGE Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
4.1.1.2 More belongs to the cupin superfamily, bicupin Bacillus subtilis
4.1.1.2 YoaN
-
 Bacillus subtilis
4.1.1.2 YvrK
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.2 26
-
 assay at Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.2 54
-
 oxalate pH 5, 26°C, recombinant YvrK Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.2 5
-
 assay at Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.2 O2 requirement, both Mn2+ and O2 are cofactors acting together as a two-electron sink during catalysis Bacillus subtilis