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Literature summary for 1.11.1.21 extracted from

  • Vlasits, J.; Jakopitsch, C.; Schwanninger, M.; Holubar, P.; Obinger, C.
    Hydrogen peroxide oxidation by catalase-peroxidase follows a non-scrambling mechanism (2007), FEBS Lett., 581, 320-324.
    View publication on PubMed
Search for more literature for 1.11.1.21

Protein Variants

Protein Variants Comment Organism
D152S mutant with very low catalase activity Synechocystis sp.
H123E mutant with very low catalase activity Synechocystis sp.
R439A mutant with very low catalase activity Synechocystis sp.
W122F mutant without catalase activity Synechocystis sp.
Y249F mutant with very low catalase activity Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-
Synechocystis sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2O2
-
 Mycobacterium tuberculosis O2 + H2O
-
 ?
H2O2
-
 Synechocystis sp. O2 + H2O
-
 ?

Synonyms

Synonyms Comment Organism
KatG
-
 Mycobacterium tuberculosis
KatG
-
 Synechocystis sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2
-
 H2O2 catalase activity, mutant enzyme H123E, in 100 mM phosphate buffer, pH 7.0, at 23°C Synechocystis sp.
6
-
 H2O2 catalase activity, mutant enzyme Y249F, in 100 mM phosphate buffer, pH 7.0, at 23°C Synechocystis sp.
170
-
 H2O2 catalase activity, mutant enzyme R439A, in 100 mM phosphate buffer, pH 7.0, at 23°C Synechocystis sp.
200
-
 H2O2 catalase activity, mutant enzyme D152S, in 100 mM phosphate buffer, pH 7.0, at 23°C Synechocystis sp.
3500
-
 H2O2 catalase activity, wild type enzyme, in 100 mM phosphate buffer, pH 7.0, at 23°C Synechocystis sp.
6000
-
 H2O2 catalase activity, wild type enzyme, in 100 mM phosphate buffer, pH 7.0, at 23°C Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
heme
-
 Mycobacterium tuberculosis
heme
-
 Synechocystis sp.