| Description | Catalases ( ) are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects [ ]. 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 () that are closely related to plant peroxidases, and non-haem, manganese-containing catalases ( ) that are found in bacteria [ ]. 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 [, ].Structurally, catalases are composed of a long amino-terminal arm, an antiparallel eight-stranded β-barrel, an extended wrapping loop, a four-helical domain and, in large catalases, a carboxy-terminal domain with flavodoxin-like topology joined by a long loop [ ]. This entry represents the helical domain found in clade 2 of the mono-functional, haem-containing catalases. | Name | Catalase, mono-functional, haem-containing, clade 2, helical domain |
| Short Name | Catalase_clade2_helical | Type | Homologous_superfamily |
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