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Literature summary extracted from

  • Anand, R.; Dorrestein, P.C.; Kinsland, C.; Begley, T.P.; Ealick, S.E.
    Structure of oxalate decarboxylase from Bacillus subtilis at 1.75 A resolution (2002), Biochemistry, 41, 7659-7669.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.1.2 additional information not induced by oxalate, but acid induced Bacillus subtilis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.2 yvrK gene, expression in Escherichia coli B834 (DE3) Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.2 recombinant OXDC, 3-dimensional structures in absence of formate and complexed with formate, hanging drop vapor diffusion technique, X-ray analysis Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.2 E333A mutant of the Mn-binding site in domain II, 25fold reduced formate production, 4fold reduced CO2 production Bacillus subtilis
4.1.1.2 R270E mutant with 20fold reduced CO2 production Bacillus subtilis
4.1.1.2 Y340F mutant with 13fold reduced CO2 production Bacillus subtilis

General Stability

EC Number General Stability Organism
4.1.1.2 unstable enzyme, loses activity during purification, undergoes partial precipitation during assays Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.2 oxalate substrate inhibition Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.2 15
-
oxalate
-
Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.2 Mn2+ metalloenzyme, Mn2+-dependent, each cupin domain contains one Mn-binding site that is buried deeply inside the beta-barrel, 2 binding sites within a monomer, mode of binding, mechanism Bacillus subtilis
4.1.1.2 additional information enzyme contains an additional unidentified metal binding site on the enzyme surface, modeled as Mg2+ Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.2 264000
-
-
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
-
formate + CO2
-
?
4.1.1.2 oxalate + H+ Bacillus subtilis 168 / CU1065
-
formate + CO2
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.2 Bacillus subtilis O34714
-
-
4.1.1.2 Bacillus subtilis 168 / CU1065 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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.2 oxalate + H+
-
Bacillus subtilis formate + CO2
-
?
4.1.1.2 oxalate + H+ OXDC acts exclusively on oxalate, Glu-333 of the second Mn-binding site serves as a proton donor in the production of formate, catalytic mechanism, enzyme structure Bacillus subtilis formate + CO2
-
?
4.1.1.2 oxalate + H+
-
Bacillus subtilis 168 / CU1065 formate + CO2
-
?
4.1.1.2 oxalate + H+ OXDC acts exclusively on oxalate, Glu-333 of the second Mn-binding site serves as a proton donor in the production of formate, catalytic mechanism, enzyme structure Bacillus subtilis 168 / CU1065 formate + CO2
-
?

Subunits

EC Number Subunits Comment Organism
4.1.1.2 homohexamer monomeric and hexameric structure 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 OXDC
-
Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.2 additional information
-
CO2 assay at room temperature Bacillus subtilis
4.1.1.2 37
-
formate assay 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
-
Bacillus subtilis

pH Optimum

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

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.1.1.2 3 7.5 70% of maximum activity at pH 3, no activity at pH 7.5 Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.2 additional information no requirement for any organic cofactor Bacillus subtilis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
4.1.1.2 Bacillus subtilis predicted value
-
5.1
4.1.1.2 Bacillus subtilis experimentally determined value
-
6.1