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
- donor + H2O2 ⇌ oxidized donor + 2 H2O
- 2 H2O2 ⇌ O2 + 2 H2O
| Catalase-peroxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 | ||||||||
| |||||||||
This enzyme is a strong catalase with H2O2 as donor which releases O2.
References
edit- ^ Loewen PC, Triggs BL, George CS, Hrabarchuk BE (May 1985). "Genetic mapping of katG, a locus that affects synthesis of the bifunctional catalase-peroxidase hydroperoxidase I in Escherichia coli". Journal of Bacteriology. 162 (2): 661–7. doi:10.1128/JB.162.2.661-667.1985. PMC 218901. PMID 3886630.
- ^ Hochman A, Goldberg I (April 1991). "Purification and characterization of a catalase-peroxidase and a typical catalase from the bacterium Klebsiella pneumoniae". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1077 (3): 299–307. doi:10.1016/0167-4838(91)90544-a. PMID 2029529.
- ^ Fraaije MW, Roubroeks HP, Hagen WR, Van Berkel WJ (January 1996). "Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimum". European Journal of Biochemistry. 235 (1–2): 192–8. CiteSeerX 10.1.1.317.1785. doi:10.1111/j.1432-1033.1996.00192.x. PMID 8631329.
- ^ Bertrand T, Eady NA, Jones JN, Nagy JM, Jamart-Grégoire B, Raven EL, Brown KA (September 2004). "Crystal structure of Mycobacterium tuberculosis catalase-peroxidase". The Journal of Biological Chemistry. 279 (37): 38991–9. doi:10.1074/jbc.M402382200. PMID 15231843.
- ^ Vlasits J, Jakopitsch C, Bernroitner M, Zamocky M, Furtmüller PG, Obinger C (August 2010). "Mechanisms of catalase activity of heme peroxidases". Archives of Biochemistry and Biophysics. 500 (1): 74–81. doi:10.1016/j.abb.2010.04.018. PMID 20434429.
External links
edit- Catalase-peroxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
