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MetaCyc Reaction: 1.11.1.21

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 1.11.1.21

Enzymes and Genes:

Escherichia coli K-12 substr. MG1655: hydroperoxidase IInferred from experiment: katG

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: catalase-peroxidase

Enzyme Commission Synonyms: katG (gene name)

Taxonomic Range: Archaea, Fungi, Bacteria

Enzyme Commission Summary:
Differs from EC 1.11.1.7, peroxidase in having a relatively high catalase ( EC 1.11.1.6) 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.

Citations: [Loewen85, Hochman91, Fraaije96, Bertrand04, Vlasits10]

Gene-Reaction Schematic

Gene-Reaction Schematic

Unification Links: KEGG:R03532

Relationship Links: BRENDA:EC:1.11.1.21, ENZYME:EC:1.11.1.21, IUBMB-ExplorEnz:EC:1.11.1.21

Credits:
Revised 13-Sep-2012 by Caspi R, SRI International


References

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

Vlasits10: Vlasits J, Jakopitsch C, Bernroitner M, Zamocky M, Furtmuller PG, Obinger C (2010). "Mechanisms of catalase activity of heme peroxidases." Arch Biochem Biophys 500(1);74-81. PMID: 20434429


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Tue May 3, 2016, biocyc14.