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 highs amounts of spermine, the aldehydic groups formed upon oxidation of spermine by...

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Bibliographic Details
Published in:	Biochemistry and molecular biology international Vol. 41; no. 2; pp. 407 - 413
Main Authors:	Padiglia, A, Medda, R, Paci, M, Sette, M, Lorrai, A, Floris, G
Format:	Journal Article
Language:	English
Published:	UK Informa Healthcare 01-02-1997
Subjects:	Amine oxidase amine oxidase (copper-containing) Copper Fabaceae - enzymology Lens culinaris Lens esculenta Lentil Magnetic Resonance Spectroscopy Mass Spectrometry Oxidation-Reduction Oxidoreductases Acting on CH-NH Group Donors - metabolism Plants, Medicinal Pyrimidines - biosynthesis Spermine Spermine - metabolism
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Summary:	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 highs 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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1039-9712 1521-6543 1521-6551
DOI:	10.1080/15216549700201421