Oxidation of spermine by an amine oxidase from lentil seedlings

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-HCl buffer; the Km value is 4.4-10-4 molar, similar to that found with other substrates (putrescine and spermidine).