ExplorEnz: EC 1.11.1.21

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1.11.1.21

Accepted name:

catalase-peroxidase

Reaction:

(1) donor + H₂O₂ = oxidized donor + 2 H₂O
(2) 2 H₂O₂ = O₂ + 2 H₂O

Other name(s):

katG (gene name)

Systematic name:

donor:hydrogen-peroxide oxidoreductase

Comments:

Differs from EC 1.11.1.7, peroxidase in having a relatively high catalase (EC 1.11.1.6) activity with H₂O₂ as donor, releasing O₂; both activities use the same heme active site. In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Loewen, P.C., Triggs, B.L., George, C.S. and Hrabarchuk, B.E. Genetic mapping of katG, a locus that affects synthesis of the bifunctional catalase-peroxidase hydroperoxidase I in Escherichia coli. J. Bacteriol. 162 (1985) 661–667. [PMID: 3886630]
2.	Hochman, A. and Goldberg, I. Purification and characterization of a catalase-peroxidase and a typical catalase from the bacterium Klebsiella pneumoniae. Biochim. Biophys. Acta 1077 (1991) 299–307. [DOI] [PMID: 2029529]
3.	Fraaije, M.W., Roubroeks, H.P., van Berkel, W.H.J. Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimum. Eur. J. Biochem. 235 (1996) 192–198. [PMID: 8631329]
4.	Bertrand, T., Eady, N.A., Jones, J.N., Jesmin, Nagy, J.M., Jamart-Gregoire, B., Raven, E.L. and Brown, K.A. Crystal structure of Mycobacterium tuberculosis catalase-peroxidase. J. Biol. Chem. 279 (2004) 38991–38999. [DOI] [PMID: 15231843]
5.	Vlasits, J., Jakopitsch, C., Bernroitner, M., Zamocky, M., Furtmuller, P.G. and Obinger, C. Mechanisms of catalase activity of heme peroxidases. Arch. Biochem. Biophys. 500 (2010) 74–81. [DOI] [PMID: 20434429]

[EC 1.11.1.21 created 2011]