EC Number | Cloned (Comment) | Organism |
---|---|---|
1.11.1.6 | expressed in Escherichia coli Rosetta (DE3) | Ruegeria pomeroyi DSS-3 |
1.11.1.7 | expressed in Escherichia coli Rosetta (DE3) | Ruegeria pomeroyi DSS-3 |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.11.1.6 | - |
Ruegeria pomeroyi DSS-3 |
1.11.1.7 | - |
Ruegeria pomeroyi DSS-3 |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.11.1.6 | 3-Amino-1,2,4-triazole | 500 microM reduces the reactivity of catalase to 50% | Ruegeria pomeroyi DSS-3 | |
1.11.1.7 | additional information | peroxidase activity is not inhibited by 3-amino-1,2,4-triazole concentrations up to 20 mM | Ruegeria pomeroyi DSS-3 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.11.1.6 | 17.2 | - |
H2O2 | - |
Ruegeria pomeroyi DSS-3 |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.11.1.6 | 8300 | - |
ring-like arrangement of six monomers, 6 * 7900 (SDS-PAGE), 6 * 8300 calculated | Ruegeria pomeroyi DSS-3 |
1.11.1.6 | 54000 | - |
gel filtration | Ruegeria pomeroyi DSS-3 |
1.11.1.7 | 8300 | - |
ring-like arrangement of six monomers, 6 * 7900 (SDS-PAGE), 6 * 8300 calculated | Ruegeria pomeroyi DSS-3 |
1.11.1.7 | 54000 | - |
gel filtration | Ruegeria pomeroyi DSS-3 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.11.1.6 | Ruegeria pomeroyi DSS-3 | Q5LLG6 | - |
- |
1.11.1.7 | Ruegeria pomeroyi DSS-3 | Q5LLG6 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.11.1.6 | purified to homogeneity as holoprotein by affinity chromatography | Ruegeria pomeroyi DSS-3 |
1.11.1.7 | purified to homogeneity as holoprotein by affinity chromatography | Ruegeria pomeroyi DSS-3 |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.11.1.7 | additional information | - |
specific activity with o-dianisidine is 10fold lower at pH 7.5 and not measurable at higher pH values due to its instability in alkaline solution | Ruegeria pomeroyi DSS-3 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.11.1.6 | H2O2 | - |
Ruegeria pomeroyi DSS-3 | O2 + H2O | - |
? | |
1.11.1.7 | additional information | no peroxidase activity is observed with ascorbate as substrate | Ruegeria pomeroyi DSS-3 | ? | - |
? | |
1.11.1.7 | NADH + H2O2 | - |
Ruegeria pomeroyi DSS-3 | NAD+ + H2O | - |
? | |
1.11.1.7 | NADPH + H2O2 | - |
Ruegeria pomeroyi DSS-3 | NADP+ + H2O | - |
? | |
1.11.1.7 | o-dianisidine + H2O2 | - |
Ruegeria pomeroyi DSS-3 | ? + H2O | - |
? | |
1.11.1.7 | pyrogallol + H2O2 | - |
Ruegeria pomeroyi DSS-3 | purpurogallin + H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.11.1.6 | hexamer | ring-like arrangement of six monomers, 6 * 7900 (SDS-PAGE), 6 * 8300 calculated | Ruegeria pomeroyi DSS-3 |
1.11.1.7 | hexamer | ring-like arrangement of six monomers, 6 * 7900 (SDS-PAGE), 6 * 8300 calculated | Ruegeria pomeroyi DSS-3 |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.11.1.6 | HTHP | peroxidase and catalase activity | Ruegeria pomeroyi DSS-3 |
1.11.1.6 | tyrosine-coordinated heme protein | - |
Ruegeria pomeroyi DSS-3 |
1.11.1.7 | HTHP | peroxidase and catalase activity | Ruegeria pomeroyi DSS-3 |
1.11.1.7 | tyrosine-coordinated heme protein | - |
Ruegeria pomeroyi DSS-3 |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.11.1.6 | 23 | - |
highest specific activity | Ruegeria pomeroyi DSS-3 |
1.11.1.7 | 20 | - |
maximal activity | Ruegeria pomeroyi DSS-3 |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.11.1.6 | additional information | - |
high thermal stability. HTHP is stable under a wide range of temperatures. Thermal unfolding is measured up to 110°C and in the presence of high concentrations of guanidinium hydrochloride. The melting point of HTHP is estimated to be around 130°C. Catalatic activity is tested after incubation for 10 min at 85°C and 90°C and is found to be reduced by less than 5% under both conditions | Ruegeria pomeroyi DSS-3 |
1.11.1.7 | additional information | - |
high thermal stability. HTHP is stable under a wide range of temperatures. Thermal unfolding is measured up to 110°C and in the presence of high concentrations of guanidinium hydrochloride. The melting point of HTHP is estimated to be around 130°C. Catalatic activity is tested after incubation for 10 min at 85°C and 90°C and is found to be reduced by less than 5% under both conditions | Ruegeria pomeroyi DSS-3 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.11.1.6 | 10.5 | - |
highest specific activity | Ruegeria pomeroyi DSS-3 |
1.11.1.7 | 8.7 | - |
at physiological pH values the highest activity is detectable with NADH or NADPH as substrates (3.0 U/mg at pH 8.7) | Ruegeria pomeroyi DSS-3 |
1.11.1.7 | 11.7 | - |
highest peroxidase activity (25.7 U/mg), with pyrogallol as substrate | Ruegeria pomeroyi DSS-3 |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
1.11.1.6 | additional information | - |
HTHP is stable under a wide range of pH values | Ruegeria pomeroyi DSS-3 |
1.11.1.7 | additional information | - |
high thermal stability. HTHP is stable under a wide range of pH | Ruegeria pomeroyi DSS-3 |