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 hight 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., Medda, R., Paci, M., Sette, M., Lorrai, A., Fioris, G. (1997). Characterization of a cyclic compound formed after spermine oxidation by lentil amine oxidase. BIOCHEMISTRY AND MOLECULAR BIOLOGY INTERNATIONAL, 41(2), 407-413 [10.1080/15216549700201421].

Characterization of a cyclic compound formed after spermine oxidation by lentil amine oxidase

PACI, MAURIZIO;SETTE, MARCO;
1997-01-01

Abstract

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 hight 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.
1997
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
Lens esculenta; lentil; amine oxidase; copper; spermine
Padiglia, A., Medda, R., Paci, M., Sette, M., Lorrai, A., Fioris, G. (1997). Characterization of a cyclic compound formed after spermine oxidation by lentil amine oxidase. BIOCHEMISTRY AND MOLECULAR BIOLOGY INTERNATIONAL, 41(2), 407-413 [10.1080/15216549700201421].
Padiglia, A; Medda, R; Paci, M; Sette, M; Lorrai, A; Fioris, G
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/44515
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