Oxidation of spermine by an amine oxidase from lentil seedlings |
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Authors: | Cogoni A Padiglia A Medda R Segni P Floris G |
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Institution: | Istituto di Chimica Biologica, Università di Cagliari, via della Pineta, 77 09125 Cagliari, Italy. |
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Abstract: | 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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