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Literature summary extracted from

  • Burrell, M.R.; Just, V.J.; Bowater, L.; Fairhurst, S.A.; Requena, L.; Lawson, D.M.; Bornemann, S.
    Oxalate decarboxylase and oxalate oxidase activities can be interchanged with a specificity switch of up to 282,000 by mutating an active site lid (2007), Biochemistry, 46, 12327-12336.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.2 gene oxdC, expression of the C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.3.4 hanging drop vapour diffusion method solution in 50 mM Tris/HCl, pH 8.5, containing 500 mM NaCl with 4.5% (w/v) PEG 2000 Bacillus subtilis
4.1.1.2 purified recombinant enzyme, hanging drop vapor diffusion method, 0.001 m1 of 10 mg ml protein in 50 mM Tris-HCl, pH 8.5, containing 500 mM NaCl mixed with 0.001 ml of precipitant containing 4.5% w/v PEG 2000, 100 mM Tris-HCl, pH 8.5, 100 mM glycine, 5 mM DTT, and 0.5 mM MnCl2, suspended over 1 ml of precipitant at 18 °C, crystal cryoprotection by crystallization solution containing 25% w/v glycerol, X-ray diffraction structure determination and analysis at 1.80 A resolution, modelling Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
1.2.3.4 E216Q mutant exhibits a 200fold loss in decarboxylase activity and a 10fold increase in oxalate oxidase activity Bacillus subtilis
4.1.1.2 E162A/N163S/S164N site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Bacillus subtilis
4.1.1.2 additional information the decarboxylase can be converted into an oxidase by mutating amino acids of the Mn2+-binding lid that include Glu162 with specificity switches, Mn2+ content of mutant enzymes, overview Bacillus subtilis
4.1.1.2 S161D/E162A site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Bacillus subtilis
4.1.1.2 S161D/E162A/N163S site-directed mutagenesis, almost inactive mutant Bacillus subtilis
4.1.1.2 S161D/E162A/N163S/S164N site-directed mutagenesis, almost inactive mutant Bacillus subtilis
4.1.1.2 S161D/E162A/N163S/S164N/T165Q site-directed mutagenesis, almost inactive mutant Bacillus subtilis
4.1.1.2 S161D/E162S/N163S/S164N site-directed mutagenesis, almost inactive mutant Bacillus subtilis
4.1.1.2 S161D/N163S/S164N site-directed mutagenesis, the mutant shows about 60% reduced activity compared to the wild-type enzyme Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.3.4 0.55
-
oxalic acid in 50 mM succinic acid/NaOH, pH 4.0 Gelatoporia subvermispora
1.2.3.4 1.1
-
oxalic acid in 50 mM succinic acid/NaOH, pH 4.0 Hordeum vulgare
4.1.1.2 additional information
-
additional information kinetics of recombinant wild-type and mutant enzymes, overview Bacillus subtilis
4.1.1.2 2
-
oxalate pH 4.0, recombinant mutant E162A/N163S/S164N Bacillus subtilis
4.1.1.2 6.6
-
oxalate pH 4.0, recombinant wild-type enzyme Bacillus subtilis
4.1.1.2 9.1
-
oxalate pH 4.0, recombinant mutant S161D/E162A Bacillus subtilis
4.1.1.2 97
-
oxalate pH 4.0, recombinant mutant S161D/N163S/S164N Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.2 Mn2+ two manganese binding sites, Glu162 on a flexible lid is the site 1 general acid, Mn2+ content of mutant enzymes, overview 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 Bacillus subtilis
-
Formate + CO2
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.2.3.4 Bacillus subtilis
-
-
-
1.2.3.4 Gelatoporia subvermispora Q5ZH56
-
-
1.2.3.4 Hordeum vulgare P45850
-
-
4.1.1.2 Bacillus subtilis O34714 gene oxdC
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.3.4 concanavalin A affinity chromatography, carboxymethyl-Sepharose column chromatography, and gel filtration Bacillus subtilis
1.2.3.4 concanavalin A affinity chromatography, carboxymethyl-Sepharose column chromatography, and gel filtration Hordeum vulgare
1.2.3.4 concanavalin A affinity chromatography, carboxymethyl-Sepharose column chromatography, and gel filtration Gelatoporia subvermispora
4.1.1.2 recombinant C-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Bacillus subtilis

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.1.2 oxalate = formate + CO2 catalytic mechanism of oxalate decarboxylase compared to oxalate oxidase, EC 1.2.3.4 Bacillus subtilis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.3.4 root
-
Hordeum vulgare
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.3.4 oxalic acid + O2 + 2 H+
-
Bacillus subtilis 2 CO2 + H2O2
-
?
1.2.3.4 oxalic acid + O2 + 2 H+
-
Hordeum vulgare 2 CO2 + H2O2
-
?
1.2.3.4 oxalic acid + O2 + 2 H+
-
Gelatoporia subvermispora 2 CO2 + H2O2
-
?
4.1.1.2 Oxalate
-
Bacillus subtilis Formate + CO2
-
?

Synonyms

EC Number Synonyms Comment Organism
1.2.3.4 OXO
-
Hordeum vulgare
1.2.3.4 OXO-G G-isoform Gelatoporia subvermispora
4.1.1.2 More the enzyme is a member of the cupin superfamily of proteins Bacillus subtilis
4.1.1.2 OXDC
-
Bacillus subtilis

pH Optimum

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

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.2 O2
-
Bacillus subtilis