EC Number | General Stability | Organism |
---|---|---|
1.11.1.21 | both the catalatic and the peroxidatic activities are similarly inactivated by exposure to photooxidative conditions. The enzyme is reduced by sodium dithionite | Rhodobacter capsulatus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.11.1.6 | H2O2 | - |
Rhodobacter capsulatus | |
1.11.1.6 | hydroxylamine | 50% inhibition for catalase at 0.002 mM, for peroxidase at 0.078 mM | Rhodobacter capsulatus | |
1.11.1.6 | KCN | 50% inhibition of both catalase and peroxidase activities at 0.02 mM | Rhodobacter capsulatus | |
1.11.1.6 | NaN3 | 50% inhibition for catalase at 0.15 mM, for peroxidase at 0.73 mM | Rhodobacter capsulatus | |
1.11.1.21 | azide | - |
Rhodobacter capsulatus | |
1.11.1.21 | cyanide | bo th enzymic activities of catalase-peroxidase are equally inhibited by cyanide | Rhodobacter capsulatus | |
1.11.1.21 | H2O2 | both the catalatic and the peroxidatic activities are similarly inactivated by treatment with 1 mM H2O2 | Rhodobacter capsulatus | |
1.11.1.21 | hydroxylamine | - |
Rhodobacter capsulatus | |
1.11.1.21 | additional information | p-chloromercuribenzoate at concentrations up to 100 mM does not inhibit the enzyme | Rhodobacter capsulatus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.11.1.6 | 59000 | - |
4 * 59000, SDS-PAGE | Rhodobacter capsulatus |
1.11.1.6 | 236000 | - |
gel filtration | Rhodobacter capsulatus |
1.11.1.21 | 236000 | - |
gel filtration | Rhodobacter capsulatus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.11.1.6 | H2O2 | Rhodobacter capsulatus | bifunctional catalase-peroxidase | O2 + H2O | - |
? |
EC Number | Organic Solvent | Comment | Organism |
---|---|---|---|
1.11.1.21 | chloroform | both the catalatic and the peroxidatic activities are similarly inactivated by exposure to chloroform | Rhodobacter capsulatus |
1.11.1.21 | Ethanol | both the catalatic and the peroxidatic activities are similarly inactivated by exposure to ethanol | Rhodobacter capsulatus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.11.1.6 | Rhodobacter capsulatus | - |
- |
- |
1.11.1.21 | Rhodobacter capsulatus | - |
- |
- |
EC Number | Oxidation Stability | Organism |
---|---|---|
1.11.1.6 | sensitive to photooxidation | Rhodobacter capsulatus |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.11.1.6 | to homogeneity, chromatography techniques | Rhodobacter capsulatus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.11.1.6 | cell culture | - |
Rhodobacter capsulatus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.11.1.6 | 3,3'-diaminobenzidine + H2O2 | - |
Rhodobacter capsulatus | ? + H2O | - |
? | |
1.11.1.6 | H2O2 | bifunctional catalase-peroxidase | Rhodobacter capsulatus | O2 + H2O | - |
? | |
1.11.1.6 | o-dianisidine + H2O2 | - |
Rhodobacter capsulatus | ? + H2O | - |
? | |
1.11.1.6 | pyrogallol + H2O2 | - |
Rhodobacter capsulatus | ? + H2O | - |
? | |
1.11.1.21 | diaminobenzidine + H2O2 | - |
Rhodobacter capsulatus | oxidized diaminobenzidine + H2O | - |
? | |
1.11.1.21 | H2O2 | - |
Rhodobacter capsulatus | O2 + H2O | - |
? | |
1.11.1.21 | additional information | no reaction is detected with guaiacol or with ascorbate | Rhodobacter capsulatus | ? | - |
? | |
1.11.1.21 | o-dianisidine + H2O2 | - |
Rhodobacter capsulatus | oxidized o-dianisidine + H2O | - |
? | |
1.11.1.21 | pyrogallol + H2O2 | - |
Rhodobacter capsulatus | ? + H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.11.1.6 | tetramer | 4 * 59000, SDS-PAGE | Rhodobacter capsulatus |
1.11.1.21 | homotetramer | - |
Rhodobacter capsulatus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.11.1.6 | 50 | - |
loss of both catalase-peroxidase activities | Rhodobacter capsulatus |
1.11.1.21 | 50 | - |
both the catalatic and the peroxidatic activities are similarly inactivated by heating to 50°C | Rhodobacter capsulatus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.11.1.21 | 5 | 5.3 | peroxidatic activity | Rhodobacter capsulatus |
1.11.1.21 | 6 | 6.5 | catalatic activity | Rhodobacter capsulatus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.11.1.6 | heme | 1-1.2 protoheme IX per tetramer | Rhodobacter capsulatus | |
1.11.1.21 | heme | there are 1-1.2 molecules of protoheme IX per tetrameric molecule | Rhodobacter capsulatus |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
1.11.1.21 | Rhodobacter capsulatus | isoelectric focusing | - |
4.5 |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
1.11.1.21 | 0.00215 | - |
catalatic activity, in 100 mM potassium phosphate, pH 6.3, at 30°C | Rhodobacter capsulatus | hydroxylamine | |
1.11.1.21 | 0.022 | - |
catalatic activity, in 100 mM potassium phosphate, pH 6.3, at 30°C | Rhodobacter capsulatus | cyanide | |
1.11.1.21 | 0.023 | - |
peroxidatic activity, in 100 mM potassium phosphate, pH 5.2, at 30°C | Rhodobacter capsulatus | cyanide | |
1.11.1.21 | 0.078 | - |
peroxidatic activity, in 100 mM potassium phosphate, pH 5.2, at 30°C | Rhodobacter capsulatus | hydroxylamine | |
1.11.1.21 | 0.15 | - |
catalatic activity, in 100 mM potassium phosphate, pH 6.3, at 30°C | Rhodobacter capsulatus | azide | |
1.11.1.21 | 0.73 | - |
peroxidatic activity, in 100 mM potassium phosphate, pH 5.2, at 30°C | Rhodobacter capsulatus | azide |