EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.2 | O2 | requires catalytic dioxygen for activity | Bacillus subtilis |
EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.1.2 | yvrk gene, expression in Escherichia coli BL21(DE3) | Bacillus subtilis |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.1.1.2 | - |
Bacillus subtilis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.1.2 | additional information | - |
additional information | kinetic data, kinetic mechanism | Bacillus subtilis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.2 | Mn2+ | contains Mn2+ in its resting state and two Mn-binding sites, may be only the C-terminal binding site is catalytically active, the N-terminal site not, manganese in the active site can abstract an electron from bound substrate | Bacillus subtilis |
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 | - |
? | |
4.1.1.2 | oxalate + H+ | Bacillus subtilis 168 | - |
formate + CO2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.2 | Bacillus subtilis | - |
- |
- |
4.1.1.2 | Bacillus subtilis 168 | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.1.2 | recombinant OXDC | Bacillus subtilis |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
4.1.1.2 | oxalate = formate + CO2 | detailed catalytic mechanism, kinetic mechanism | Bacillus subtilis |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
4.1.1.2 | additional information | - |
- |
Bacillus subtilis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.2 | oxalate + H+ | - |
Bacillus subtilis | formate + CO2 | - |
? | |
4.1.1.2 | oxalate + H+ | mechanism, multistep model in which a reversible, proton-coupled, electron transfer from bound oxalate to the Mn-enzyme gives an oxalate radical, which decarboxylates to yield a formate radical anion, subsequent reduction and protonation of this intermediate then gives formate, irreversible decarboxylation step, no net redox change between substrate and products, roles of Arg-270 and Glu-333 in catalysis | Bacillus subtilis | formate + CO2 | - |
? | |
4.1.1.2 | oxalate + H+ | - |
Bacillus subtilis 168 | formate + CO2 | - |
? | |
4.1.1.2 | oxalate + H+ | mechanism, multistep model in which a reversible, proton-coupled, electron transfer from bound oxalate to the Mn-enzyme gives an oxalate radical, which decarboxylates to yield a formate radical anion, subsequent reduction and protonation of this intermediate then gives formate, irreversible decarboxylation step, no net redox change between substrate and products, roles of Arg-270 and Glu-333 in catalysis | Bacillus subtilis 168 | formate + CO2 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.1.2 | More | member of the cupin superfamily | Bacillus subtilis |
4.1.1.2 | OXDC | - |
Bacillus subtilis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.1.2 | 21 | 22 | assay at | Bacillus subtilis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.1.1.2 | additional information | - |
pH-dependence of OxDC activity | Bacillus subtilis |