Biology:Catalase-peroxidase
From HandWiki
| Catalase-peroxidase | |||||||||
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| 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 | ||||||||
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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
This enzyme is a strong catalase with H2O2 as donor which releases O2.
References
- ↑ "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. May 1985. doi:10.1128/JB.162.2.661-667.1985. PMID 3886630.
- ↑ "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. April 1991. doi:10.1016/0167-4838(91)90544-a. PMID 2029529.
- ↑ "Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimum". European Journal of Biochemistry 235 (1–2): 192–8. January 1996. doi:10.1111/j.1432-1033.1996.00192.x. PMID 8631329.
- ↑ "Crystal structure of Mycobacterium tuberculosis catalase-peroxidase". The Journal of Biological Chemistry 279 (37): 38991–9. September 2004. doi:10.1074/jbc.M402382200. PMID 15231843.
- ↑ "Mechanisms of catalase activity of heme peroxidases". Archives of Biochemistry and Biophysics 500 (1): 74–81. August 2010. doi:10.1016/j.abb.2010.04.018. PMID 20434429.
External links
- Catalase-peroxidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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