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Literature summary for 1.11.1.21 extracted from

  • Tichy, M.; Vermaas, W.
    In vivo role of catalase-peroxidase in Synechocystis sp. strain PCC 6803 (1999), J. Bacteriol., 181, 1875-1882.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.8
-
H2O2 wild type enzyme, in 25 mM HEPES-NaOH buffer (pH 7.0) at 25°C Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp. P73911
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
KatG
-
Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
heme
-
Synechocystis sp.

General Information

General Information Comment Organism
malfunction although the rate of H2O2 decomposition is about 30times lower in the katG deletion mutant than in the wild type, the strain has a normal phenotype and its doubling time as well as its resistance to H2O2 and methyl viologen are indistinguishable from those of the wild type Synechocystis sp.
physiological function catalase-peroxidase has a protective role against environmental H2O2 Synechocystis sp.