EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.1.2 | expressed in Escherichia coli BL21(DE3) cells | Bacillus subtilis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.1.1.2 | E101A | the mutant shows strongly decreased activity | Bacillus subtilis |
4.1.1.2 | E101D | the mutant shows strongly decreased activity | Bacillus subtilis |
4.1.1.2 | E101Q | the mutant shows strongly decreased activity | Bacillus subtilis |
4.1.1.2 | E101Q/E280Q | the mutant shows strongly decreased activity | Bacillus subtilis |
4.1.1.2 | E280A | the mutant shows strongly decreased activity | Bacillus subtilis |
4.1.1.2 | E280D | the mutant shows strongly decreased activity | Bacillus subtilis |
4.1.1.2 | E280Q | the mutant shows strongly decreased activity | Bacillus subtilis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.1.2 | 2.9 | - |
oxalate | mutant enzyme E101A , in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 2.9 | - |
oxalate | mutant enzyme E101Q/E280Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 3 | - |
oxalate | mutant enzyme E280A , in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 3.4 | - |
oxalate | mutant enzyme E101D, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 4 | - |
oxalate | mutant enzyme E101Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 5.4 | - |
oxalate | mutant enzyme E280D, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 8.4 | - |
oxalate | wild type enzyme, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 10.1 | - |
oxalate | mutant enzyme E280Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.2 | Mn2+ | the enzyme is composed of two cupin domains, each of which contains a Mn2+ ion, OxDC activity is linearly correlated with manganese content, untagged enzyme samples exhibit a metal content of 1.8 Mn2+ per monomer | Bacillus subtilis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.2 | Bacillus subtilis | O34714 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.1.2 | DEAE-Sepharose column chromatography and Phenyl-Sepharose column chromatography | Bacillus subtilis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.2 | oxalate + H+ | - |
Bacillus subtilis | CO2 + formate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.1.2 | OXDC | - |
Bacillus subtilis |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.1.2 | 0.012 | - |
oxalate | mutant enzyme E101Q/E280Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 0.019 | - |
oxalate | mutant enzyme E280A , in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 0.046 | - |
oxalate | mutant enzyme E101A , in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 0.14 | - |
oxalate | mutant enzyme E280D, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 0.49 | - |
oxalate | mutant enzyme E101D, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 0.62 | - |
oxalate | mutant enzyme E101Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 0.62 | - |
oxalate | mutant enzyme E280Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 53 | - |
oxalate | wild type enzyme, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.1.2 | 0.004 | - |
oxalate | mutant enzyme E101Q/E280Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 0.006 | - |
oxalate | mutant enzyme E280A , in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 0.016 | - |
oxalate | mutant enzyme E101A , in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 0.026 | - |
oxalate | mutant enzyme E280D, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 0.061 | - |
oxalate | mutant enzyme E280Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 0.144 | - |
oxalate | mutant enzyme E101D, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 0.155 | - |
oxalate | mutant enzyme E101Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis | |
4.1.1.2 | 6.309 | - |
oxalate | wild type enzyme, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C | Bacillus subtilis |