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The Protein Journal

, Volume 32, Issue 6, pp 435–441 | Cite as

Euphorbia characias Latex Amine Oxidase and Peroxidase: Interacting Enzymes?

  • Francesca Pintus
  • Delia Spanò
  • Giovanni Floris
  • Rosaria Medda
Article

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.

Keywords

Amines Amine oxidase Euphorbia characias Nitric oxide Peroxidase Thiocyanate 

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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Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  • Francesca Pintus
    • 1
  • Delia Spanò
    • 1
  • Giovanni Floris
    • 1
  • Rosaria Medda
    • 1
  1. 1.Department of Sciences of Life and EnvironmentUniversity of CagliariMonserratoItaly

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