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Anthranilic acid oxidase system of Tecoma stans—II. : Studies on the properties of a purified anthranilic acid oxidase system and its separation into different enzymic components

Nair, Madhusudanan P and Vaidyanathan, CS (1964) Anthranilic acid oxidase system of Tecoma stans—II. : Studies on the properties of a purified anthranilic acid oxidase system and its separation into different enzymic components. In: Phytochemistry, 3 (4). pp. 513-523.

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Official URL: http://dx.doi.org/10.1016/S0031-9422(00)88029-2

Abstract

An enzyme system which catalysed the conversion of anthranilic acid to catechol has been purified 20-fold from a cell-free leaf extract of Tecoma stans. The optimum substrate concentration was 10−3 M and optimum temperature for the reaction was 45°. The presence of a multi-enzyme system was inferred from inhibition studies. The formation of catechol was inhibited by Mg2+, Zn2+, and Co2+ ions, whereas anthranilic acid disappearance was not affected to the same extent. The effect of metal chelating agents like EDTA, cyanide and pyrophosphate showed a similar trend. PCMB inhibited catechol formation but had no effect on anthranilic acid disappearance. The reaction was not inhibited by catalase, nor was it activated by peroxide-donating systems. This ruled out the possibility of peroxidative type of reaction. The overall reaction is markedly activated by NADPH and THFA. This multi-enzyme was separated into three different components, by fractionation with Alumina Cγ and calcium phosphate gels. The overall reaction catalysed by these components can be represented as anthranilic acid→3-hydroxy anthranilic acid→o-aminophenol→catechol.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Elsevier Science.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 21 May 2010 10:39
Last Modified: 19 Sep 2010 06:07
URI: http://eprints.iisc.ernet.in/id/eprint/28006

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