Protein Variants | Comment | Organism |
---|---|---|
Y111A | the mutation leads to a 5fold reduction in the apparent kcat for catalase activity and an 8fold decrease in the apparent second-order rate constant. For peroxidase activity, the H2O2- and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)-dependent peroxidatic apparent kcat are reduced by 66% and 40%, respectively. Preparations of this variant yield a mixture of high- and low-spin heme states, thus creating the appearance of a transition between wild type (high-spin) and C-terminal lacking (low-spin) KatG | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
cyanide | - |
Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.061 | - |
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) | mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C | Escherichia coli | |
0.07 | - |
H2O2 | mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C | Escherichia coli | |
0.087 | - |
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) | wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C | Escherichia coli | |
0.18 | - |
H2O2 | wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C | Escherichia coli | |
3.5 | - |
H2O2 | wild type enzyme, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C | Escherichia coli | |
5.2 | - |
H2O2 | mutant enzyme Y111A, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
Ni-NTA column chromatography | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2 | - |
Escherichia coli | oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O | - |
? | |
H2O2 | - |
Escherichia coli | O2 + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
KatG | - |
Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
22.4 | - |
H2O2 | mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C | Escherichia coli | |
33.3 | - |
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) | mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C | Escherichia coli | |
55.2 | - |
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) | wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C | Escherichia coli | |
65 | - |
H2O2 | wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C | Escherichia coli | |
2140 | - |
H2O2 | mutant enzyme Y111A, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C | Escherichia coli | |
11000 | - |
H2O2 | wild type enzyme, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Escherichia coli |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
320 | - |
H2O2 | mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C | Escherichia coli | |
360 | - |
H2O2 | wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C | Escherichia coli | |
410 | - |
H2O2 | mutant enzyme Y111A, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C | Escherichia coli | |
546 | - |
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) | mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C | Escherichia coli | |
634 | - |
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) | wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C | Escherichia coli | |
3200 | - |
H2O2 | wild type enzyme, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C | Escherichia coli |