Anthranilic acid oxidase system of Tecomastans—III.: Studies on the conversion of o-aminophenol to catechol

Nair, P Madhusudanan and Rao, PV Subba and Vaidyanathana, CS (1966) Anthranilic acid oxidase system of Tecomastans—III.: Studies on the conversion of o-aminophenol to catechol. In: Phytochemistry, 5 (6). pp. 1317-1321. (In Press)

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Abstract

The terminal step in the oxidation of anthranilic acid to catechol by anthranilic acid oxidase system from Tecoma stans, which converts o-aminophenol to catechol has been studied in detail. The reaction catalyses the conversion of one molecule of o-aminophenol to one molecule each of ammonia and catechol. The partially purified enzyme has a pH optimum of 6·2 in citrate-phosphate buffer and a temperature optimum of 45°. The metal ions, Mg2+, Co2+ and Fe3+ were inhibitory to the reaction. Metal chelating agents like 8-hydroxyquinoline, o-phenanthroline, and diethyldithiocarbamate, caused a high degree of inhibition. A sulfhydryl requirement for the reaction was inferred from the inhibition of the reaction by p-chloromercuribenzoate and its reversal with GSH. Atebrin inhibition was reversed by addition of FAD to the reaction mixture.

Item Type:	Journal Article
Publication:	Phytochemistry
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	17 May 2010 09:07
Last Modified:	19 Sep 2010 06:06
URI:	http://eprints.iisc.ac.in/id/eprint/27871

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