Inhibition of pig liver and Zea mays L. polyamine oxidase: A comparative study

R. Federico, L. Leone, M. Botta, C. Binda, R. Angelini, G. Venturini, P. Ascenzi

Research output: Contribution to journalArticlepeer-review

Abstract

Polyamine oxidase (PAO) is involved in polyamine metabolism and production of hydrogen peroxide in animal and plants, thus representing a key system in development and programmed cell death. In the present study, the inhibitory effect of amiloride, p-aminobenzamidine, clonidine, 4′,6-diamidino-2-phenyl-indole (DAPI), gabexate mesylate, guazatine, and N,N′-bis(2,3-butadienyl)-1,4-butane-diamine (MDL72527) on the catalytic activity of pig liver and Zea mays L. PAO, Lens culinaris L. and Pisum sativum L. and swine kidney copper amine oxidase, bovine trypsin, as well as neuronal constitutive nitric oxide synthase (NOS-I) was investigated. Moreover, agmatine and N3-prenylagmatine (G3) were observed to inhibit pig liver and Zea mays L. PAO, bovine trypsin, and NOS-I action, but were substrates for Lens culinaris L., Pisum sativum L. and swine kidney copper amine oxidase. Guazatine and G3 inhibited selectively Zea mays L. PAO with Ki values of 7.5 × 10-9 M and 1.5 × 10-8 M, respectively (at pH 6.5 and 25.0°C). As a whole, the data reported here represent examples of enzyme cross-inhibition, and appear to be relevant in view of the use of cationic L-arginine-and imidazole-based compounds as drugs.

Original languageEnglish
Pages (from-to)147-155
Number of pages9
JournalJournal of Enzyme Inhibition
Volume16
Issue number2
Publication statusPublished - 2001

Keywords

  • Lens culinaris L. copper amine oxidase
  • Pig liver polyamine oxidase
  • Zea mays L. polyamine oxidase

ASJC Scopus subject areas

  • Molecular Medicine
  • Biochemistry
  • Drug Discovery
  • Pharmacology

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