Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.11.1.21 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

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

Inhibitors Comment Organism Structure
cyanide
-
Synechocystis sp.

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
-
-

Specific Activity [micromol/min/mg]

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

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

Synonyms

Synonyms Comment Organism
KatG
-
Synechocystis sp.

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
heme
-
Synechocystis sp.

kcat/KM [mM/s]

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