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Literature summary for 1.11.1.21 extracted from

  • Zhao, X.; Yu, S.; Ranguelova, K.; Suarez, J.; Metlitsky, L.; Schelvis, J.P.; Magliozzo, R.S.
    Role of the oxyferrous heme intermediate and distal side adduct radical in the catalase activity of Mycobacterium tuberculosis KatG revealed by the W107F mutant (2009), J. Biol. Chem., 284, 7030-7037.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli cells Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
M255A the mutant exhibits severely reduced catalase activity compared to the wild type enzyme Mycobacterium tuberculosis
W107F the mutant exhibits severely reduced catalase activity yet normal peroxidase activity and contains more abundant 6-coordinate heme in high spin and low spin forms compared to the wild type enzyme Mycobacterium tuberculosis
Y229F the mutant exhibits severely reduced catalase activity compared to the wild type enzyme Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WIE5
-
-
Mycobacterium tuberculosis H37Rv P9WIE5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2O2
-
Mycobacterium tuberculosis O2 + H2O
-
?
H2O2
-
Mycobacterium tuberculosis H37Rv O2 + H2O
-
?
o-dianisidine + H2O2
-
Mycobacterium tuberculosis ?
-
?
o-dianisidine + H2O2
-
Mycobacterium tuberculosis H37Rv ?
-
?
tert-butyl peroxide + H2O2
-
Mycobacterium tuberculosis ?
-
?
tert-butyl peroxide + H2O2
-
Mycobacterium tuberculosis H37Rv ?
-
?

Synonyms

Synonyms Comment Organism
catalase-peroxidase
-
Mycobacterium tuberculosis
KatG
-
Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
heme
-
Mycobacterium tuberculosis