|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 188.8.131.52
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: Balanced.
Enzyme Commission Primary Name: catalase-peroxidase
Enzyme Commission Synonyms: katG (gene name)
Enzyme Commission Summary:
Differs from EC 184.108.40.206, peroxidase in having a relatively high catalase (EC 220.127.116.11) activity with hydrogen peroxide as donor, releasing oxygen; both activities use the same heme active site. In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid.
Unification Links: KEGG:R03532
Bertrand04: Bertrand T, Eady NA, Jones JN, Jesmin , Nagy JM, Jamart-Gregoire B, Raven EL, Brown KA (2004). "Crystal structure of Mycobacterium tuberculosis catalase-peroxidase." J Biol Chem 279(37);38991-9. PMID: 15231843
Fraaije96: Fraaije MW, Roubroeks HP, Hagen WR, Van Berkel WJ (1996). "Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimum." Eur J Biochem 235(1-2);192-8. PMID: 8631329
Hochman91: Hochman A, Goldberg I (1991). "Purification and characterization of a catalase-peroxidase and a typical catalase from the bacterium Klebsiella pneumoniae." Biochim Biophys Acta 1077(3);299-307. PMID: 2029529
Loewen85: Loewen PC, Triggs BL, George CS, Hrabarchuk BE (1985). "Genetic mapping of katG, a locus that affects synthesis of the bifunctional catalase-peroxidase hydroperoxidase I in Escherichia coli." J Bacteriol 1985;162(2);661-7. PMID: 3886630
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