Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzyme in strain PCC 6803 | Synechocystis sp. PCC 6803 |
Protein Variants | Comment | Organism |
---|---|---|
D152N | site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction, reduced catalase activity and increased peroxidase activity compared to the wild-type enzyme | Synechocystis sp. PCC 6803 |
D152S | site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction, reduced catalase activity and increased peroxidase activity compared to the wild-type enzyme | Synechocystis sp. PCC 6803 |
D152W | site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction, highly reduced catalase activity and highly increased peroxidase activity compared to the wild-type enzyme | Synechocystis sp. PCC 6803 |
D402E | site-directed mutagenesis, residue of the heme binding pocket proximal side, mutation effect on heme structure and residue interaction, reduced catalase and peroxidase activity compared to the wild-type enzyme | Synechocystis sp. PCC 6803 |
D402N | site-directed mutagenesis, residue of the heme binding pocket proximal side, mutation effect on heme structure and residue interaction, reduced catalase and peroxidase activity compared to the wild-type enzyme | Synechocystis sp. PCC 6803 |
H290Q | site-directed mutagenesis, residue of the heme binding pocket proximal side, mutation effect on heme structure and residue interaction, highly reduced catalase and peroxidase activity compared to the wild-type enzyme | Synechocystis sp. PCC 6803 |
N153A | site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction | Synechocystis sp. PCC 6803 |
N153D | site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction | Synechocystis sp. PCC 6803 |
P151A | site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction, slightly reduced catalase and peroxidase activity compared to the wild-type enzyme | Synechocystis sp. PCC 6803 |
W341A | site-directed mutagenesis, residue of the heme binding pocket proximal side, mutation effect on heme structure and residue interaction, highly reduced catalase and peroxidase activity compared to the wild-type enzyme | Synechocystis sp. PCC 6803 |
W341F | site-directed mutagenesis, residue of the heme binding pocket proximal side, mutation effect on heme structure and residue interaction, 50% reduced catalase activity and 50% increased peroxidase activity compared to the wild-type enzyme, binds completely to NaF | Synechocystis sp. PCC 6803 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.4 | - |
H2O2 | mutant D152S, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
2.5 | - |
H2O2 | mutants D152N and P151A, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
3.2 | - |
H2O2 | mutant D152W, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
4.1 | - |
H2O2 | wild-type enzyme, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
4.3 | - |
H2O2 | mutant W341A, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
5.9 | - |
H2O2 | mutant D402E, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
6.3 | - |
H2O2 | mutant W341F, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
6.4 | - |
H2O2 | mutant D402N, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
15 | - |
H2O2 | mutant H290Q, pH 7.0, 30°C | Synechocystis sp. PCC 6803 |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | enzyme contains heme | Synechocystis sp. PCC 6803 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
H2O2 | Synechocystis sp. PCC 6803 | - |
O2 + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Synechocystis sp. PCC 6803 | - |
gene katG, KatG is a bifunctional enzyme showing both catalase and peroxidase activities | - |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzyme from strain PCC 6803 | Synechocystis sp. PCC 6803 |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.18 | - |
substrate o-dianisidine, mutant H290Q | Synechocystis sp. PCC 6803 |
0.8 | - |
substrate o-dianisidine, mutant W341A | Synechocystis sp. PCC 6803 |
1.8 | - |
substrate o-dianisidine, mutant D402N | Synechocystis sp. PCC 6803 |
2.1 | - |
substrate o-dianisidine, mutant D402E | Synechocystis sp. PCC 6803 |
2.4 | - |
substrate o-dianisidine, mutant P151A | Synechocystis sp. PCC 6803 |
3.2 | - |
substrate o-dianisidine, wild-type enzyme | Synechocystis sp. PCC 6803 |
6.1 | - |
substrate o-dianisidine, mutant W341F | Synechocystis sp. PCC 6803 |
7.5 | - |
substrate o-dianisidine, mutant D152N | Synechocystis sp. PCC 6803 |
7.6 | - |
substrate o-dianisidine, mutant D152S | Synechocystis sp. PCC 6803 |
21.5 | - |
substrate o-dianisidine, mutant D152W | Synechocystis sp. PCC 6803 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
H2O2 | - |
Synechocystis sp. PCC 6803 | O2 + H2O | - |
? | |
H2O2 | catalase activity | Synechocystis sp. PCC 6803 | O2 + H2O | - |
? | |
H2O2 + o-dianisidine | peroxidase activity | Synechocystis sp. PCC 6803 | ? | - |
? | |
additional information | bifunctional enzyme showing both catalase and peroxidase activities | Synechocystis sp. PCC 6803 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
catalase-peroxidase | - |
Synechocystis sp. PCC 6803 |
KatG | - |
Synechocystis sp. PCC 6803 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Synechocystis sp. PCC 6803 |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3 | - |
H2O2 | mutant H290Q, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
16 | - |
H2O2 | mutant W341A, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
17 | - |
H2O2 | mutant D402N, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
20 | - |
H2O2 | mutant D152W, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
21 | - |
H2O2 | mutant D402E, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
95 | - |
H2O2 | mutant D152N, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
200 | - |
H2O2 | mutant D152S, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
1460 | - |
H2O2 | mutant W341F, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
2500 | - |
H2O2 | mutant P151A, pH 7.0, 30°C | Synechocystis sp. PCC 6803 | |
3500 | - |
H2O2 | wild-type enzyme, pH 7.0, 30°C | Synechocystis sp. PCC 6803 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Synechocystis sp. PCC 6803 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | binding pocket distal side: triad residues P151, D152, and N153 are important for stability, they interact with the binding pocket proximal side residues W341, D402, and H290 | Synechocystis sp. PCC 6803 |