Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.1.2 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

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

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

General Stability

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

Inhibitors

Inhibitors Comment Organism Structure
oxalate substrate inhibition Bacillus subtilis

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
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
additional information enzyme contains an additional unidentified metal binding site on the enzyme surface, modeled as Mg2+ Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
264000
-
-
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 / CU1065
-
formate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O34714
-
-
Bacillus subtilis 168 / CU1065 O34714
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant OXDC Bacillus subtilis

Reaction

Reaction Comment Organism Reaction ID
oxalate = formate + CO2 catalytic mechanism Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxalate + H+
-
Bacillus subtilis formate + CO2
-
?
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
-
?
oxalate + H+
-
Bacillus subtilis 168 / CU1065 formate + CO2
-
?
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

Subunits Comment Organism
homohexamer monomeric and hexameric structure Bacillus subtilis

Synonyms

Synonyms Comment Organism
More belongs to the cupin superfamily, bicupin Bacillus subtilis
OXDC
-
Bacillus subtilis

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
54
-
oxalate
-
Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
Bacillus subtilis

pH Range

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

Cofactor

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

pI Value

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