Comparison of kinetic properties of amine oxidases from sainfoin and lentil and immunochemical characterization of copper/quinoprotein amine oxidases

Abstract

Kinetic properties of novel amine oxidase isolated from sainfoin (Onobrychis viciifolia) were compared to those of typical plant amine oxidase (EC 1.4.3.6) from lentil (Lens culinaris). The amine oxidase from sainfoin was active toward substrates, such as 1,5‐diaminopentane (cadaverine) with Km of 0.09 mM and 1,4‐diaminobutane (putrescine) with Km of 0.24 mM. The maximum rate of oxidation for cadaverine at saturating concentration was 2.7 fold higher than that of putrescine. The amine oxidase from lentil had the maximum rate for putrescine comparable to the rate of sainfoin amine oxidase with the same substrate. Both amine oxidases, like other plant Cu‐amine oxidases, were inhibited by substrate analogs (1,5‐diamino‐3‐pentanone, 1,4‐diamino‐2‐butanone and aminoguanidine), Cu2+ chelating agents (diethyltriamine, 1,10‐phenanthroline, 8‐hydroxyquinoline, 2,2′‐bipyridyl, imidazole, sodium cyanide and sodium azide), some alkaloids (L‐lobeline and cinchonine), some lathyrogens (β‐aminopropionitrile and aminoacetonitrile) and other inhibitors (benzamide oxime, acetone oxime, hydroxylamine and pargyline). Tested by Ouchterlony's double diffusion in agarose gel, polyclonal antibodies against the amine oxidase from sainfoin, pea and grass pea cross‐reacted with amine oxidases from several other Fabaceae and from barley (Hordeum vulgare) of Poaceae, while amine oxidase from the filamentous fungus Aspergillus niger did not cross‐react at all. However, using Western blotting after SDS‐PAGE with rabbit polyclonal antibodies against the amine oxidase from Aspergillus niger, some degree of similarity of plant amine oxidases from sainfoin, pea, field pea, grass pea, fenugreek, common melilot, white sweetclover and Vicia panonica with the A. niger amine oxidase was confirmed.

An amine oxidase in seedlings of Papaver somniferum L.

“…These results for PSAO are in good agreement with the preliminary data reported by Medda et al (1995) and Peč and Frébort (1989). Aliphatic amines are the most suitable substrates for AOs from many Leguminosae for example Lens esculenta, Onobrychis viciifolia (Zajoncová et al 1999), Glycine max (Vianello et al 1993), Lathyrus sativus (Suresh et al 1976), and also for enzyme from Hyoscyamus niger, where AO takes part in biosynthesis of tropane alkaloids (Hashimoto et al 1990). As tyramine is the best substrate for AO from poppy, it indicates that this enzyme may take part in the formation of aldehyde condensation unit for the biosynthesis of (S)-reticuline in this plant.…”

An Overview of Phenylcyclopropylamine Derivatives: Biochemical and Biological Significance and Recent Developments

“…However, 2‐fluoro‐1‐phenylcyclopropylamine ( 18 ) was a weak inhibitor of tyramine oxidase, although it is a potent inhibitor of MAO . It is known that chelating compounds such as triethylenetetramine efficiently inhibit CAOs . Since the C–F bond has been reported to coordinate metal ions, a possible explanation for the inhibitory effects of these compounds could be chelation of copper with the fluorine and amino groups of the cis isomer, leading to a favored five‐membered chelate (Fig.…”

Fluorinated phenylcyclopropylamines

“…An explanation might be the ability of C-F-bonds to coordinate metal-ions [25]. In some cases, inactivation of CAOs by copper chelating agents was observed [26,27]. In the case of trans -fluoro-tranylcypromines ( cis -arrangement of fluorine and the amino group) a chelation might occur with the copper ion that is situated in the active site of tyramine oxidase.…”