Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting Functions
Use this link to cite
http://hdl.handle.net/2183/21083
Except where otherwise noted, this item's license is described as Atribución 4.0 Internacional (CC BY 4.0)
Collections
- GI-GIBE - Artigos [97]
Metadata
Show full item recordTitle
Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting FunctionsDate
2018-09-21Citation
Lüthje, S.; Martinez-Cortes, T. Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting Functions. Int. J. Mol. Sci. 2018, 19, 2876. https://doi.org/10.3390/ijms19102876
Abstract
[Abstract] Class III peroxidases are heme-containing proteins of the secretory pathway with a high redundance and versatile functions. Many soluble peroxidases have been characterized in great detail, whereas only a few studies exist on membrane-bound isoenzymes. Membrane localization of class III peroxidases has been demonstrated for tonoplast, plasma membrane and detergent resistant membrane fractions of different plant species. In silico analysis revealed transmembrane domains for about half of the class III peroxidases that are encoded by the maize (Zea mays) genome. Similar results have been found for other species like thale-cress (Arabidopsis thaliana), barrel medic (Medicago truncatula) and rice (Oryza sativa). Besides this, soluble peroxidases interact with tonoplast and plasma membranes by protein–protein interaction. The topology, spatiotemporal organization, molecular and biological functions of membrane-bound class III peroxidases are discussed. Besides a function in membrane protection and/or membrane repair, additional functions have been supported by experimental data and phylogenetics.
Keywords
Arabidopsis thaliana
Class III peroxidase
Medicago truncatula
Microdomains
Phylogenetics
Plasma membrane
Protein–protein interaction
Oryza sativa
Tonoplast
Zea mays
Class III peroxidase
Medicago truncatula
Microdomains
Phylogenetics
Plasma membrane
Protein–protein interaction
Oryza sativa
Tonoplast
Zea mays
Editor version
Rights
Atribución 4.0 Internacional (CC BY 4.0)
ISSN
1422-0067