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Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/18333

Title: Isolation and Characterization of Thielaviopsis paradoxa L-alanine Dehydrogenase
Authors: Al-Onazi, 'Mona.
Al-Dahain, 'Sooad.
El-Ansary, 'Afaf.
Marraiki, Najat.
Keywords: L-alanine, NAD+, Thielauiopsis paradoxa, sulfhydryl group, Phoenix dactylifera, deamination
Issue Date: 2011
Publisher: J Egypt Soc Parasitol
Abstract: Alanine dehydrogenase has not yet been purified from any fungal sources. The aims of this study was to isolate alanine dehydrogenase from Thielauiopsis paradoxa. The biochemical kinetic properties of the enzyme like Km, Vmax, optimum Temperature and pH were also determined. In this study, effect of certain inhibitors on the enzyme was tested. Alanine dehydrogenase (EC 1.4.1.1), an enzyme that catalyzes the reversible deamination of L-alanine in the presence of NAD+, was extracted and characterized from Thielauiopsis paradoxa, a pathogenic fungi for the date palm (Phoenix dactylifera). The enzyme showed maximal activity at pH 9.5 for the deamination of L-alanine and at pH 8.5 for the amination of pyruvate. It was active in the presence of both NAD+ and NADP+ as coenzymes for the deamination of L-alanine. In addition, the enzyme was not absolutely specific to L-alanine as a substrate in the deamination of L-alanine. L-alanine dehydrogenase had Km value for L-alanine (1.35 mM), for NAD+ 0.274 mM, NADH (0.197 mM), pyruvate (8.16 mM) and ammonia (33.5 mM). It was inhibited by Zn2+, CO" and by iodoacetate. Activation by using reduced glutathione and DTT are suggestive of sulfhydryl group participation in enzyme activity.
URI: http://hdl.handle.net/123456789/18333
ISSN: 1996-3343
Appears in Collections:College of Science

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