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Euphorbia characias Latex Amine Oxidase and Peroxidase: Interacting Enzymes?

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Abstract

This minireview deals the enzymatic transformation of some amino acids as arginine and ornithine, amines as tyramine, putrescine, spermine and spermidine, and other substances as nitric oxide and thiocyanate. These reactions, catalyzed by two proteins purified from the latex of Euphorbia characias, a copper/quinone containing amine oxidase and a cationic peroxidase, show enzymatic activity interactions probably occurring between these proteins in Euphorbia latex.

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Abbreviations

ELAO:

Euphorbia latex amine oxidase

ELP:

Euphorbia latex peroxidase

pHA:

pHydroxyphenylacetaldehyde

di-pHA:

di-pHydroxyphenylacetaldehyde

TPQ:

2,4,5-Trihydroxyphenylalanine quinone

Tyr:

Tyramine

diTyr:

di-Tyramine

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Authors and Affiliations

  1. Department of Sciences of Life and Environment, University of Cagliari, 09042, Monserrato, CA, Italy

    Francesca Pintus, Delia Spanò, Giovanni Floris & Rosaria Medda

Authors
  1. Francesca Pintus
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  2. Delia Spanò
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  3. Giovanni Floris
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  4. Rosaria Medda
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Corresponding author

Correspondence to Rosaria Medda.

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Pintus, F., Spanò, D., Floris, G. et al. Euphorbia characias Latex Amine Oxidase and Peroxidase: Interacting Enzymes?. Protein J 32, 435–441 (2013). https://doi.org/10.1007/s10930-013-9501-6

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  • DOI: https://doi.org/10.1007/s10930-013-9501-6

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