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Literature summary extracted from

  • Jakopitsch, C.; Auer, M.; Regelsberger, G.; Jantschko, W.; Furtmüller, P.; Rüker, F.; Obinger, C.
    The catalytic role of the distal site asparagine-histidine couple in catalase-peroxidases (2003), Eur. J. Biochem., 270, 1006-1013.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.21 N153A the mutant shows 6% of wild type catalase activity and exhibits an overall peroxidase activity similar with wild type KatG Synechocystis sp.
1.11.1.21 N153D the mutant shows 16.5% of wild type catalase activity and exhibits an overall peroxidase activity similar with wild type KatG Synechocystis sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.11.1.21 cyanide
-
 Synechocystis sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.1.21 1.7
-
 H2O2 catalase activity, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C Synechocystis sp.
1.11.1.21 2.3
-
 H2O2 catalase activity, mutant enzyme N153D, in 50 mM phosphate buffer, pH 7.0, and 30°C Synechocystis sp.
1.11.1.21 4.1
-
 H2O2 catalase activity, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C Synechocystis sp.

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.21 Synechocystis sp.
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.11.1.21 0.55
-
 peroxidase activity, using guaiacol as substrate, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C Synechocystis sp.
1.11.1.21 0.6
-
 peroxidase activity, using guaiacol as substrate, mutant enzyme N153D, in 50 mM phosphate buffer, pH 7.0, and 30°C Synechocystis sp.
1.11.1.21 0.6
-
 peroxidase activity, using guaiacol as substrate, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C Synechocystis sp.
1.11.1.21 1.9
-
 peroxidase activity, using o-dianisidine as substrate, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C Synechocystis sp.
1.11.1.21 3.8
-
 peroxidase activity, using o-dianisidine as substrate, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C Synechocystis sp.
1.11.1.21 4.3
-
 peroxidase activity, using o-dianisidine as substrate, mutant enzyme N153D, in 50 mM phosphate buffer, pH 7.0, and 30°C Synechocystis sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.21 guaiacol + H2O2
-
 Synechocystis sp. tetraguaiacol + H2O
-
 ?
1.11.1.21 H2O2
-
 Synechocystis sp. O2 + H2O
-
 ?
1.11.1.21 o-dianisidine + H2O2
-
 Synechocystis sp. oxidized o-dianisidine + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.11.1.21 KatG
-
 Synechocystis sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.11.1.21 200
-
 H2O2 catalase activity, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C Synechocystis sp.
1.11.1.21 580
-
 H2O2 catalase activity, mutant enzyme N153D, in 50 mM phosphate buffer, pH 7.0, and 30°C Synechocystis sp.
1.11.1.21 3500
-
 H2O2 catalase activity, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C Synechocystis sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.11.1.21 6.5
-
-
 Synechocystis sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.21 heme
-
 Synechocystis sp.

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.11.1.21 120
-
 H2O2 catalase activity, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C Synechocystis sp.
1.11.1.21 250
-
 H2O2 catalase activity, mutant enzyme N153D, in 50 mM phosphate buffer, pH 7.0, and 30°C Synechocystis sp.
1.11.1.21 850
-
 H2O2 catalase activity, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C Synechocystis sp.