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Literature summary extracted from

  • Just, V.J.; Stevenson, C.E.M.; Bowater, L.; Tanner, A.; Lawson, D.M.; Bornemann, S.
    A closed conformation of Bacillus subtilis oxalate decarboxylase OxdC provides evidence for the true identity of the active site (2004), J. Biol. Chem., 279, 19867-19874.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.1.2 additional information induced by low pH, not by oxalate salts Bacillus subtilis

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.2 recombinant OxdC, hanging drop vapour diffusion method, X-ray analysis Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.2 E162A Mn2+-binding site 1 mutant, inactive Bacillus subtilis
4.1.1.2 E162Q Mn2+-binding site 1 mutant, Vmax and kcat/Km is 1% that of wild-type Bacillus subtilis
4.1.1.2 E333A Mn2+-binding site 2 mutant, 4-6% of wild-type activity at pH 4, lower Km for oxalate, kcat/Km is 25% that of wild-type Bacillus subtilis
4.1.1.2 E333Q Mn2+-binding site 2 mutant, inactive Bacillus subtilis
4.1.1.2 R270A Mn2+-binding site 2 mutant, kcat/Km is 3% that of wild-type Bacillus subtilis
4.1.1.2 R270K Mn2+-binding site 2 mutant, kcat/Km is 43% that of wild-type Bacillus subtilis
4.1.1.2 R92A Mn2+-binding site 1 mutant, inactive Bacillus subtilis
4.1.1.2 R92K Mn2+-binding site 1 mutant, kcat/Km is 7% that of wild-type Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.2 1
-
 oxalate pH 4, 26°C, R270K mutant OxdC Bacillus subtilis
4.1.1.2 2
-
 oxalate pH 4, 26°C, R92K mutant OxdC Bacillus subtilis
4.1.1.2 4
-
 oxalate pH 4, 26°C, E333A mutant OxdC Bacillus subtilis
4.1.1.2 8
-
 oxalate pH 4, 26°C, R270A mutant OxdC Bacillus subtilis
4.1.1.2 14
-
 oxalate pH 4, 26°C, E162Q mutant OxdC Bacillus subtilis
4.1.1.2 16.4
-
 oxalate pH 4, 26°C, wild-type OxdC Bacillus subtilis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.1.1.2 cytoplasm
-
 Bacillus subtilis 5737
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.2 Mn2+ contains 2 Mn2+ per subunit, role in catalysis, mechanism, 2 Mn-binding sites, the N-terminal Mn-binding site 1 is catalytically active 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 involved in the elevation of cytoplasmic pH formate + CO2
-
 ?
4.1.1.2 oxalate + H+ Bacillus subtilis 168 involved in the elevation of cytoplasmic pH formate + CO2
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.2 recombinant OXDC Bacillus subtilis

Reaction

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.2 oxalate + H+ catalytic mechanism involves the requirement of an active site proton donor: Glu-162, catalytic cycle, enzyme structure, N-terminal domain is the catalytically active domain, dioxygen-dependent reaction involves no net redox change Bacillus subtilis formate + CO2
-
 ?
4.1.1.2 oxalate + H+ involved in the elevation of cytoplasmic pH Bacillus subtilis formate + CO2
-
 ?
4.1.1.2 oxalate + H+ catalytic mechanism involves the requirement of an active site proton donor: Glu-162, catalytic cycle, enzyme structure, N-terminal domain is the catalytically active domain, dioxygen-dependent reaction involves no net redox change Bacillus subtilis 168 formate + CO2
-
 ?
4.1.1.2 oxalate + H+ involved in the elevation of cytoplasmic pH Bacillus subtilis 168 formate + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.2 More enzyme belongs to the cupin superfamily, bicupin Bacillus subtilis
4.1.1.2 OXDC formerly 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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.2 4
-
 assay at Bacillus subtilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.1.1.2 7.5
-
 not active above Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.2 O2 utilizes dioxygen as cofactor Bacillus subtilis