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Calcium Ions and a Secreted Peroxidase in Euphorbia characias Latex are Made for Each Other

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Abstract

This minireview deals of a protein, a class III secreted peroxidase, present as unique isoform in the latex of the perennial Mediterranean shrub Euphorbia characias. The paper reports on the molecular properties, on the structures (primary, secondary and tertiary), and on the catalytic mechanism of this enzyme. Here is also reported the extraordinary effect of calcium ions on the structure and on the enzyme activity of Euphorbia peroxidase. These ions can either enhance the catalytic efficiency of the enzyme toward some substrates or can regulate the ability of the enzyme to execute different metabolic pathways toward the same substrate. This review will give a valuable reference to the peroxidase fans and the general readers will find many thorough suggestions for future researches giving birth to new studies and important discoveries.

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Abbreviations

ABTS:

2,2′-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)

ELAO:

Euphorbia latex amine oxidase

ELP:

Euphorbia latex peroxidase

HRP:

horseradish peroxidase

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Acknowledgments

This study was partially supported by a grant from “Fondazione Banco di Sardegna”, Sassari, and from Regione Autonoma della Sardegna, Progetti di Ricerca di Base CRP2-22.

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Authors and Affiliations

  1. Department of Applied Sciences in Biosystems, University of Cagliari, Cagliari, Italy

    Francesca Pintus, Delia Spanò, Rosaria Medda & Giovanni Floris

  2. Dipartimento di Scienze Applicate ai Biosistemi, Cittadella Universitaria, 09042, Monserrato, CA, Italy

    Giovanni Floris

Authors
  1. Francesca Pintus
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  2. Delia Spanò
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  3. Rosaria Medda
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  4. Giovanni Floris
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Correspondence to Giovanni Floris.

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Pintus, F., Spanò, D., Medda, R. et al. Calcium Ions and a Secreted Peroxidase in Euphorbia characias Latex are Made for Each Other. Protein J 30, 115–123 (2011). https://doi.org/10.1007/s10930-011-9310-8

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  • DOI: https://doi.org/10.1007/s10930-011-9310-8

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