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 |
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 |
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 |
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 |
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 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.2 | Oxalate | Bacillus subtilis | - |
Formate + CO2 | - |
? |
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 | - |
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 |
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 |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.2.3.4 | root | - |
Hordeum vulgare | - |
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 | - |
? |
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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.1.1.2 | 4 | - |
assay at | Bacillus subtilis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.2 | O2 | - |
Bacillus subtilis |