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Cogoni A, Padiglia A, Medda R, et al. Oxidation of spermine by an amine oxidase from lentil seedlings. Plant Physiol. 1991;95(2):477-9doi: 10.1104/pp.95.2.477.
Cogoni, A., Padiglia, A., Medda, R., Segni, P., & Floris, G. (1991). Oxidation of spermine by an amine oxidase from lentil seedlings. Plant physiology, 95(2), 477-9. https://doi.org/10.1104/pp.95.2.477
Cogoni, A, et al. "Oxidation of spermine by an amine oxidase from lentil seedlings." Plant physiology vol. 95,2 (1991): 477-9. doi: https://doi.org/10.1104/pp.95.2.477
Cogoni A, Padiglia A, Medda R, Segni P, Floris G. Oxidation of spermine by an amine oxidase from lentil seedlings. Plant Physiol. 1991 Feb;95(2):477-9. doi: 10.1104/pp.95.2.477. PMID: 16668008; PMCID: PMC1077555.
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Plant Physiol. 1991 Feb;95(2):477-9. doi: 10.1104/pp.95.2.477.

Oxidation of spermine by an amine oxidase from lentil seedlings.

Plant physiology

A Cogoni, A Padiglia, R Medda, P Segni, G Floris

Affiliations

  1. Istituto di Chimica Biologica, Università di Cagliari, via della Pineta, 77 09125 Cagliari, Italy.

PMID: 16668008 PMCID: PMC1077555 DOI: 10.1104/pp.95.2.477

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 K(m) value is 4.4.10(-4) molar, similar to that found with other substrates (putrescine and spermidine).

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