Catalase-peroxidase

Catalase-peroxidase
Identifiers
EC number 1.11.1.21
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Catalase-peroxidase (EC 1.11.1.21, katG (gene)) is an enzyme with systematic name donor:hydrogen-peroxide oxidoreductase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

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

This enzyme is a strong catalase with H2O2 as donor which releases O2.

References

  1. Loewen, P.C.; Triggs, B.L.; George, C.S.; Hrabarchuk, B.E. (1985). "Genetic mapping of katG, a locus that affects synthesis of the bifunctional catalase-peroxidase hydroperoxidase I in Escherichia coli". J. Bacteriol. 162 (2): 661–667. PMC 218901Freely accessible. PMID 3886630.
  2. 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. doi:10.1016/0167-4838(91)90544-a. PMID 2029529.
  3. Fraaije, M.W.; Roubroeks, H.P.; van Berkel, W.H.J. (1996). "Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimum". Eur. J. Biochem. 235 (1-2): 192–198. doi:10.1111/j.1432-1033.1996.00192.x. PMID 8631329.
  4. Bertrand, T.; Eady, N.A.; Jones, J.N.; Jesmin, Nagy J.M.; Jamart-Gregoire, B.; Raven, E.L.; Brown, K.A. (2004). "Crystal structure of Mycobacterium tuberculosis catalase-peroxidase". J. Biol. Chem. 279 (37): 38991–38999. doi:10.1074/jbc.M402382200. PMID 15231843.
  5. Vlasits, J.; Jakopitsch, C.; Bernroitner, M.; Zamocky, M.; Furtmuller, P.G.; Obinger, C. (2010). "Mechanisms of catalase activity of heme peroxidases". Arch. Biochem. Biophys. 500 (1): 74–81. doi:10.1016/j.abb.2010.04.018. PMID 20434429.

External links

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