EC 1.11.1.21 - Catalase peroxidase

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IntEnz Enzyme Nomenclature
EC 1.11.1.21

Names

Accepted name:
catalase peroxidase
Other name:
katG (gene name)
Systematic name:
donor:hydrogen-peroxide oxidoreductase

Reactions

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (342) [show] [UniProt]

References

  1. Loewen, P. C., Triggs, B. L., George, C. S., 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: 661-667 (1985). [PMID: 3886630]
  2. Hochman, A., Goldberg, I.
    Purification and characterization of a catalase-peroxidase and a typical catalase from the bacterium Klebsiella pneumoniae.
    Biochim. Biophys. Acta 1077: 299-307 (1991). [PMID: 2029529]
  3. Fraaije, M. W., Roubroeks, H. P., Hagen, W. R., Van Berkel, W. J.
    Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimum.
    Eur. J. Biochem. 235: 192-198 (1996). [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: 38991-38999 (2004). [PMID: 15231843]
  5. Vlasits, J., Jakopitsch, C., Bernroitner, M., Zamocky, M., Furtmuller, P. G., Obinger, C.
    Mechanisms of catalase activity of heme peroxidases.
    Arch. Biochem. Biophys. 500: 74-81 (2010). [PMID: 20434429]

[EC 1.11.1.21 created 2011]