Member database | Pfam |
Pfam type | domain |
Short name | Catalase |
Author | Finn RD;0000-0001-8626-2148 |
Sequence Ontology | 0000417 |
Description Imported from IPR011614
Catalases (
1.11.1.6) are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects
[1]. Hydrogen peroxide is produced as a consequence of oxidative cellular metabolism and can be converted to the highly reactive hydroxyl radical via transition metals, this radical being able to damage a wide variety of molecules within a cell, leading to oxidative stress and cell death. Catalases act to neutralise hydrogen peroxide toxicity, and are produced by all aerobic organisms ranging from bacteria to man. Most catalases are mono-functional, haem-containing enzymes, although there are also bifunctional haem-containing peroxidase/catalases (
IPR000763) that are closely related to plant peroxidases, and non-haem, manganese-containing catalases (
IPR007760) that are found in bacteria
[2]. Based on a phylogenetic analysis, catalases can be classified into clade 1, 2 and 3. Clade 1 contains small subunit catalases from plants and a subset of bacteria; clade 2 contains large subunit catalases from fungi and a second subset of bacteria; and clade 3 contains small subunit catalases from bacteria, fungi, protists, animals, and plants
[3, 4].
This entry represent the core-forming domain of mono-functional, haem-containing catalases. It does not cover the region that carries an immune-responsive amphipathic octa-peptide that is found in the C-terminal of some catalases (
IPR010582).
References Imported from IPR011614
1.Mitochondrial catalase and oxidative injury. Bai J, Cederbaum AI. 10, 189-99, (2001). PMID: 11351128
2.Diversity of structures and properties among catalases. Chelikani P, Fita I, Loewen PC. Cell. Mol. Life Sci. 61, 192-208, (2004). View articlePMID: 14745498
3.Phylogenetic relationships among prokaryotic and eukaryotic catalases. Klotz MG, Klassen GR, Loewen PC. Mol. Biol. Evol. 14, 951-8, (1997). PMID: 9287428
4.Structure of the Clade 1 catalase, CatF of Pseudomonas syringae, at 1.8 A resolution. Carpena X, Soriano M, Klotz MG, Duckworth HW, Donald LJ, Melik-Adamyan W, Fita I, Loewen PC. Proteins 50, 423-36, (2003). View articlePMID: 12557185