Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 95:477-479 (1991)
© 1991 American Society of Plant Biologists

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Metabolism and Enzymology

Oxidation of Spermine by an Amine Oxidase from Lentil Seedlings

Antonina Cogoni, Alessandra Padiglia, Rosaria Medda, Paolo Segni and Giovanni Floris

Istituto di Chimica Biologica, Università di Cagliari, via della Pineta, 77 09125 Cagliari, Italy

Spermine is a substrate of lentil (Lens culinaris) seedling amine oxidase and the oxidation products are reversible inactivators of the enzyme. The spermine is oxidized at the terminal amino groups to a dialdehyde: 2 moles of hydrogen peroxide and 2 moles of ammonia per mole of spermine are formed. The pH optimum of the enzyme with spermine is 7.9 in TI-HCI buffer; the Km value is 4.4·10–4 molar, similar to that found with other substrates (putrescine and spermidine).






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Copyright © 1991 by the American Society of Plant Biologists