F
IPR040333

Catalase, clade 3

InterPro entry
Short nameCatalase_3
Overlapping
homologous
superfamilies
 
family relationships

Description

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
[6]
. 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
[1]
. 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
[2, 3]
.

Clade 3 catalases are the most abundant subfamily and are found in all three kingdoms of life; they have a relatively small subunit size of 43 to 75kDa, and bind a protoheme IX (heme b) group buried deep inside the structure. Clade 3 catalases also bind NADPH as a second redox-active cofactor. They form tetramers, and in eukaryotic cells, catalases are located in peroxisomes
[4, 5]
.

References

1.Diversity of structures and properties among catalases. Chelikani P, Fita I, Loewen PC. Cell. Mol. Life Sci. 61, 192-208, (2004). View articlePMID: 14745498

2.Phylogenetic relationships among prokaryotic and eukaryotic catalases. Klotz MG, Klassen GR, Loewen PC. Mol. Biol. Evol. 14, 951-8, (1997). PMID: 9287428

3.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

4.Evolution of catalases from bacteria to humans. Zamocky M, Furtmuller PG, Obinger C. Antioxid. Redox Signal. 10, 1527-48, (2008). View articlePMID: 18498226

5.Thirty years of heme catalases structural biology. Diaz A, Loewen PC, Fita I, Carpena X. Arch. Biochem. Biophys. 525, 102-10, (2012). View articlePMID: 22209752

6.Mitochondrial catalase and oxidative injury. Bai J, Cederbaum AI. 10, 189-99, (2001). PMID: 11351128

GO terms

Cross References

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