EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.2 | additional information | not induced by oxalate, but acid induced | Bacillus subtilis |
EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.1.2 | yvrK gene, expression in Escherichia coli B834 (DE3) | Bacillus subtilis |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.1.1.2 | recombinant OXDC, 3-dimensional structures in absence of formate and complexed with formate, hanging drop vapor diffusion technique, X-ray analysis | Bacillus subtilis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.1.1.2 | E333A | mutant of the Mn-binding site in domain II, 25fold reduced formate production, 4fold reduced CO2 production | Bacillus subtilis |
4.1.1.2 | R270E | mutant with 20fold reduced CO2 production | Bacillus subtilis |
4.1.1.2 | Y340F | mutant with 13fold reduced CO2 production | Bacillus subtilis |
EC Number | General Stability | Organism |
---|---|---|
4.1.1.2 | unstable enzyme, loses activity during purification, undergoes partial precipitation during assays | Bacillus subtilis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.2 | oxalate | substrate inhibition | Bacillus subtilis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.1.2 | 15 | - |
oxalate | - |
Bacillus subtilis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.2 | Mn2+ | metalloenzyme, Mn2+-dependent, each cupin domain contains one Mn-binding site that is buried deeply inside the beta-barrel, 2 binding sites within a monomer, mode of binding, mechanism | Bacillus subtilis | |
4.1.1.2 | additional information | enzyme contains an additional unidentified metal binding site on the enzyme surface, modeled as Mg2+ | Bacillus subtilis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
4.1.1.2 | 264000 | - |
- |
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 / CU1065 | - |
formate + CO2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.2 | Bacillus subtilis | O34714 | - |
- |
4.1.1.2 | Bacillus subtilis 168 / CU1065 | O34714 | - |
- |
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 | catalytic mechanism | 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+ | OXDC acts exclusively on oxalate, Glu-333 of the second Mn-binding site serves as a proton donor in the production of formate, catalytic mechanism, enzyme structure | Bacillus subtilis | formate + CO2 | - |
? | |
4.1.1.2 | oxalate + H+ | - |
Bacillus subtilis 168 / CU1065 | formate + CO2 | - |
? | |
4.1.1.2 | oxalate + H+ | OXDC acts exclusively on oxalate, Glu-333 of the second Mn-binding site serves as a proton donor in the production of formate, catalytic mechanism, enzyme structure | Bacillus subtilis 168 / CU1065 | formate + CO2 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.1.1.2 | homohexamer | monomeric and hexameric structure | Bacillus subtilis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.1.2 | More | belongs to the cupin superfamily, bicupin | Bacillus subtilis |
4.1.1.2 | OXDC | - |
Bacillus subtilis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.1.2 | additional information | - |
CO2 assay at room temperature | Bacillus subtilis |
4.1.1.2 | 37 | - |
formate assay | Bacillus subtilis |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.1.2 | 54 | - |
oxalate | - |
Bacillus subtilis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.1.1.2 | 5 | - |
- |
Bacillus subtilis |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
4.1.1.2 | 3 | 7.5 | 70% of maximum activity at pH 3, no activity at pH 7.5 | Bacillus subtilis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.2 | additional information | no requirement for any organic cofactor | Bacillus subtilis |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
4.1.1.2 | Bacillus subtilis | predicted value | - |
5.1 |
4.1.1.2 | Bacillus subtilis | experimentally determined value | - |
6.1 |