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Literature summary extracted from
- Real-time monitoring of the oxalate decarboxylase reaction and probing hydron exchange in the product, formate, using fourier transform infrared spectroscopy (2006), Biochemistry, 45, 10667-10673.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.1.1.2 | gene oxdC, expression of C-terminally His-tagged OxdC in Escherichia coli strain BL21(DE3) | Bacillus subtilis |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.1.1.2 | additional information | - |
additional information | Fourier transform infrared spectroscopy to monitor in real time both substrate consumption and product formation, the Km for oxalate determined using this assay is 3.8fold lower than that estimated from a stopped assay, overview, solvent deuterium kinetic isotope effect, overview | Bacillus subtilis |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.1.2 | Mn2+ | - |
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 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.1.2 | Bacillus subtilis | - |
gene oxdC | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.1.1.2 | recombinant C-terminally His-tagged OxdC from Escherichia coli strain BL21(DE3) | Bacillus subtilis |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.2 | additional information | - |
two assay methods, stopped assay and Fourier transform infrared spectroscopy to monitor in real time both substrate consumption and product formation | Bacillus subtilis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.1.2 | additional information | the enzyme also shows oxalate oxidase activity, catalytic cycle, overview | Bacillus subtilis | ? | - |
? | |
| 4.1.1.2 | oxalate + H+ | - |
Bacillus subtilis | formate + CO2 | - |
? | |
| 4.1.1.2 | oxalate + H+ | catalytic cycle, overview, the enzyme converts oxalate to formate and carbon dioxide, via an enzyme-bound formyl radical catalytic intermediate, and uses dioxygen as a cofactor despite the reaction involving no net redox change, overview, a proton transfer event occurs during a rate-limiting step, hydron exchange in formate, semiempirical quantum mechanical calculation, overview | Bacillus subtilis | formate + CO2 | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 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 | 25 | - |
stopped assay at | Bacillus subtilis |
| 4.1.1.2 | 26 | - |
Fourier transformation infrared spectroscopic assay at | Bacillus subtilis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.2 | 4 | - |
stopped assay at | Bacillus subtilis |
| 4.1.1.2 | 5 | - |
Fourier transformation infrared spectroscopic assay at | Bacillus subtilis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.1.2 | O2 | - |
Bacillus subtilis | |
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