Inhibition of chickpea seedling copper amine oxidases by tetraethylenepentamine

Talaei, S. and Asadi , A. and Amani , M. (2012) Inhibition of chickpea seedling copper amine oxidases by tetraethylenepentamine. Molecular Biology Research Communications, 1 (1). pp. 27-32.

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Copper amine oxidases are important enzymes, which contribute to the regulation of mono- and polyamine levels. Each monomer contains one Cu(II) ion and 2,4,5-trihydroxyphenylalanine (TPQ) as cofactors. They catalyze the oxidative deamination of primary amines to aldehydes with a ping-pong mechanism consisting of a transamination. The mechanism is followed by the transfer of two electrons to molecular oxygen which is reduced to hydrogen peroxide. Inhibitors are important tools in the study of catalytic properties of copper amine oxidases and they also have a wide application in physiological research. In this study, purification of the chickpea seedling amine oxidase, was done via salting out by ammonium sulfate and dialysis, followed by DEAE-cellulose column chromatography. By using the Lineweaver - Burk plot, the Km and Vm of the enzyme were found to be 3.3 mM and 0.95 mmol/min/mg, respectively. In this study, the interaction of chickpea diamino oxidase with tetraethylene- pentamine was studied. Analysis of kinetic data indicated that tetraethylenepentamine (with Ki=0.1 mM) inhibits the enzyme by linear mixed inhibitory effect.

Item Type: Article
Author Affiliation: University of Mohaghegh Ardabili, Ardabil, Iran, University of Medical science, Ardabil, Iran
Subjects: Crop Improvement
Plant Physiology and Biochemistry > Biochemistry
Divisions: Chickpea
Depositing User: Mr. SanatKumar Behera
Date Deposited: 27 Aug 2012 07:25
Last Modified: 27 Aug 2012 07:26
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