InterPro : IPR007760

Name  Manganese catalase Short Name  Mn_catalase
Type  Family Description  Catalases () are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen. 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. There are three structurally independent classes of catalases: ubiquitous mono-functional haem-containing catalases (), bifunctional haem-containing catalase-peroxidases that are closely related to plant peroxidases (), and non-haem manganese-containing catalases [].This entry represents the non-haem Mn-catalases, which are found in several bacterial species []. The structure of the Mn catalase from Lactobacillus plantarumreveals a homo-hexamer, where each subunit contains a dimanganese active site that is accessed by a single substrate channel []. The dimanganese active site performs a two-electron catalytic cycle that alternately oxidises and reduces the dimanganese atoms in a manner that is similar to its haem-counterpart found in other catalases.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

1 Contains

Id Name Short Name Type
IPR012347 Ferritin-related Ferritin-rel Domain

0 Found In

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Chelikani P Diversity of structures and properties among catalases. 2004 Cell Mol Life Sci 61 192-208
Barynin VV Crystal structure of manganese catalase from Lactobacillus plantarum. 2001 Structure 9 725-38
Wu AJ Structural, spectroscopic, and reactivity models for the manganese catalases. 2004 Chem Rev 104 903-38



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)