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Literature summary for 1.11.1.21 extracted from

  • Jakopitsch, C.; Auer, M.; Regelsberger, G.; Jantschko, W.; Furtmuller, P.G.; Ruker, F.; Obinger, C.
    Distal site aspartate is essential in the catalase activity of catalase-peroxidases (2003), Biochemistry, 42, 5292-5300.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli Synechocystis sp.

Protein Variants

Protein Variants Comment Organism
D152N site-directed mutagenesis, 2.7% remaining catalase activity and 2-7times higher peroxidase activity compared to the wild-type enzyme, highly altered pH profile Synechocystis sp.
D152S site-directed mutagenesis, 5.7% remaining catalase activity and 2-7times higher peroxidase activity compared to the wild-type enzyme, highly altered pH profile Synechocystis sp.
D152W site-directed mutagenesis, 0.6% remaining catalase activity and 2-7times higher peroxidase activity compared to the wild-type enzyme, highly altered pH profile Synechocystis sp.
P151A site-directed mutagenesis, slightly increased catalase activity compared to the wild-type enzyme Synechocystis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady- and transient-state kinetics Synechocystis sp.
2.4
-
H2O2 mutant D152S, pH 7.0, 30°C Synechocystis sp.
2.5
-
H2O2 mutants D152N and P151A, pH 7.0, 30°C Synechocystis sp.
3.2
-
H2O2 mutant D152W, pH 7.0, 30°C Synechocystis sp.
4.1
-
H2O2 wild-type enzyme, pH 7.0, 30°C Synechocystis sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ heme Synechocystis sp.

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
strain PCC 6803
-

Reaction

Reaction Comment Organism Reaction ID
2 H2O2 = O2 + 2 H2O distal site Asp152 is essential for the catalase activity of catalase-peroxidase, mechanism for hydrogen peroxide oxidation in volving residues Trp122 and Asp152 Synechocystis sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.5
-
substrate guajacol, mutant P151A Synechocystis sp.
0.6
-
substrate guajacol, wild-type enzyme Synechocystis sp.
2.4
-
substrate o-dianisidine, mutant P151A Synechocystis sp.
2.5
-
substrate guajacol, mutants D152N and D152S Synechocystis sp.
3.2
-
substrate o-dianisidine, wild-type enzyme Synechocystis sp.
4.1
-
substrate guajacol, mutant D152W Synechocystis sp.
4.1
-
substrate pyrogallol, mutant P151A Synechocystis sp.
6.6
-
substrate pyrogallol, wild-type enzyme Synechocystis sp.
7.3
-
substrate pyrogallol, mutant D152W Synechocystis sp.
7.5
-
substrate o-dianisidine, mutant D152N Synechocystis sp.
7.6
-
substrate o-dianisidine, mutant D152S Synechocystis sp.
12.5
-
substrate pyrogallol, mutant D152N Synechocystis sp.
13.6
-
substrate pyrogallol, mutant D152S Synechocystis sp.
21.5
-
substrate o-dianisidine, mutant D152W Synechocystis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
guajacol + H2O2 peroxidase activity Synechocystis sp. ? + H2O
-
?
H2O2
-
Synechocystis sp. O2 + H2O
-
?
H2O2 catalase activity Synechocystis sp. O2 + H2O
-
?
additional information bifunctional enzyme providing catalase and peroxidase activities, intermediate structure Synechocystis sp. ?
-
?
o-dianisidine + H2O2 peroxidase activity Synechocystis sp. ? + H2O
-
?
pyrogallol + H2O2 peroxidase activity Synechocystis sp. ? + H2O
-
?

Synonyms

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
20
-
H2O2 mutant D152W, pH 7.0, 30°C Synechocystis sp.
95
-
H2O2 mutant D152N, pH 7.0, 30°C Synechocystis sp.
200
-
H2O2 mutant D152S, pH 7.0, 30°C Synechocystis sp.
2500
-
H2O2 mutant P151A, pH 7.0, 30°C Synechocystis sp.
3500
-
H2O2 wild-type enzyme, pH 7.0, 30°C Synechocystis sp.

pH Optimum

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