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Literature summary for 1.11.1.21 extracted from

  • Santoni, E.; Jakopitsch, C.; Obinger, C.; Smulevich, G.
    Comparison between catalase-peroxidase and cytochrome c peroxidase. The role of the hydrogen-bond network for protein stability and catalysis (2004), Biochemistry, 43, 5792-5802.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzyme in strain PCC 6803 Synechocystis sp. PCC 6803

Protein Variants

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 [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

Metals/Ions Comment Organism Structure
Fe2+ enzyme contains heme Synechocystis sp. PCC 6803

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
H2O2 Synechocystis sp. PCC 6803
-
O2 + H2O
-
?

Organism

Organism UniProt Comment Textmining
Synechocystis sp. PCC 6803
-
gene katG, KatG is a bifunctional enzyme showing both catalase and peroxidase activities
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzyme from strain PCC 6803 Synechocystis sp. PCC 6803

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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

Synonyms Comment Organism
catalase-peroxidase
-
Synechocystis sp. PCC 6803
KatG
-
Synechocystis sp. PCC 6803

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Synechocystis sp. PCC 6803

Turnover Number [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Synechocystis sp. PCC 6803

Cofactor

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