Cloned (Comment) | Organism |
---|---|
gene oxdC, expression of the C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Bacillus subtilis |
Crystallization (Comment) | Organism |
---|---|
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 | Comment | Organism |
---|---|---|
E162A/N163S/S164N | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Bacillus subtilis |
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 |
S161D/E162A | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Bacillus subtilis |
S161D/E162A/N163S | site-directed mutagenesis, almost inactive mutant | Bacillus subtilis |
S161D/E162A/N163S/S164N | site-directed mutagenesis, almost inactive mutant | Bacillus subtilis |
S161D/E162A/N163S/S164N/T165Q | site-directed mutagenesis, almost inactive mutant | Bacillus subtilis |
S161D/E162S/N163S/S164N | site-directed mutagenesis, almost inactive mutant | Bacillus subtilis |
S161D/N163S/S164N | site-directed mutagenesis, the mutant shows about 60% reduced activity compared to the wild-type enzyme | Bacillus subtilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of recombinant wild-type and mutant enzymes, overview | Bacillus subtilis | |
2 | - |
oxalate | pH 4.0, recombinant mutant E162A/N163S/S164N | Bacillus subtilis | |
6.6 | - |
oxalate | pH 4.0, recombinant wild-type enzyme | Bacillus subtilis | |
9.1 | - |
oxalate | pH 4.0, recombinant mutant S161D/E162A | Bacillus subtilis | |
97 | - |
oxalate | pH 4.0, recombinant mutant S161D/N163S/S164N | Bacillus subtilis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Oxalate | Bacillus subtilis | - |
Formate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | O34714 | gene oxdC | - |
Purification (Comment) | Organism |
---|---|
recombinant C-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus subtilis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
oxalate = formate + CO2 | catalytic mechanism of oxalate decarboxylase compared to oxalate oxidase, EC 1.2.3.4 | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Oxalate | - |
Bacillus subtilis | Formate + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
More | the enzyme is a member of the cupin superfamily of proteins | Bacillus subtilis |
OXDC | - |
Bacillus subtilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4 | - |
assay at | Bacillus subtilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
O2 | - |
Bacillus subtilis |