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Theoretical and Experimental Plant Physiology

On-line version ISSN 2197-0025


BARROS, Raimundo Santos et al. Detection of 1-aminocyclopropane-1-carboxylate oxidase activity in seeds of Stylosanthes humilis H.B.K. Theor. Exp. Plant Physiol. [online]. 2013, vol.25, n.3, pp.231-239. ISSN 2197-0025.

The activity of 1-aminocyclopropane-1-carboxylate oxidase (ACO) was characterized in seeds of the tropical legume Townsville stylo (Stylosanthes humilis) both in vitro (desalted extract of non-dormant seeds) and in vivo (entire dormant seeds). Optimum conditions for maximum in vitro ACO activity in a Trizma-HCl 100 mM buffered medium were: pH 7.0, temperature 32ºC and cofactors and co-substrate at the following concentrations: NaHCO3 30 mM, sodium ascorbate 30 mM and FeSO4 50 µM. Rates of in vitro reaction catalyzed by ACO were shown to be constant within the interval 15-150 minutes from the onset of the reaction. The apparent Km for in vitro ACO, as determined from the non-linear curve fitting to the Michaelis-Menten equation, was 156±8.3 µM ACC with a Vmax 5.4±0.08 mmol (ET) g-1 h-1 on a fresh matter (FM) basis. In vivo (control basal medium: HCl-KOH 10 mM pH 7.0, 30ºC, reaction time 15 hours) apparent Km was 230±27 µM ACC and Vmax 11.9±0.38 mmol (ET) g-1.h-1 on a FM basis. These data suggest that the enzyme exhibits a relatively low affinity for the substrate. The well-known inhibitors of ACO activity, α-aminoisobutyric acid, salicylic and acetylsalicylic acids, n-propylgallate and cobaltous ions, were highly effective in inhibiting ACO activity of Townsville stylo seeds.

Keywords : dioxygenase; enzymatic kinetics; ethylene; inhibition; ACO.

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