Characterization of a cyclic compound formed after spermine oxidation by lentil amine oxidase.
Spermine is a substrate of lentil seedling amine oxidase and is oxidized at terminal amino groups to a dialdehyde: 2 mol of hydrogen peroxide and two mol of ammonia per mol of spermine are formed. In the presence of high amounts of spermine, the aldehydic groups formed upon oxidation of spermine by the enzyme, may react with primary amino groups of free spermine leading to the formation of aromatic pyrimidinic ring after beta-elimination at secondary amino groups.
Padiglia
A
A
Institute of Biological Chemistry, University of Cagliari, Italy.
Medda
R
R
Paci
M
M
Sette
M
M
Lorrai
A
A
Floris
G
G
D006631:Amine Oxidase (Copper-Containing); D007887:Fabaceae / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D010084:Oxidation-Reduction; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism*; D010946:Plants, Medicinal; D011743:Pyrimidines / Q000096:biosynthesis*; D013096:Spermine / Q000378:metabolism*
D011743:Pyrimidines; D013096:Spermine; D006631:Amine Oxidase (Copper-Containing); D000587:Oxidoreductases Acting on CH-NH Group Donors