2,3-Dihydroxybenzoate 2,3-oxygenase from the chloroplast fraction of Tecoma stans

Sharma, Harmesh K and Vaidyanathan, Chelakara S (1975) 2,3-Dihydroxybenzoate 2,3-oxygenase from the chloroplast fraction of Tecoma stans. In: Phytochemistry, 14 (10). pp. 2135-2139.

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Abstract

2,3-Dihydroxybenzoate-2,3-oxygenase is mainly localized in the soluble and the chloroplast fractions of Tecoma leaves. It is associated with the lamellar structure of the chloroplast fraction. The chloroplast enzyme has properties similar to those of the soluble enzyme, but it has a longer half-life and is more stable to dialysis than the soluble enzyme. It is inhibited by sulfhydryl reagents and the inhibition is reversed by the addition of reduced glutathione. The chloroplast enzyme is insensitive to iron-chelating agents. The enzyme loses activity on dialysis against copper-chelating agents and the activity is completely recovered on the addition of copper; addition of iron does not restore the activity. Polyphenol oxidase is probably present only in the active form in the Tecoma chloroplast but it is not involved in the intradiol cleavage of 2,3-dihydroxybenzoic acid.

Item Type:	Journal Article
Publication:	Phytochemistry
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Keywords:	Tecoma stans;Bignoniaceae;2,3-dihydroxybenzoate 2,3-oxygenase;chloroplast;enzyme properties;metal ion requirement;polyphenol oxidase.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	06 Oct 2009 03:20
Last Modified:	19 Sep 2010 05:47
URI:	http://eprints.iisc.ac.in/id/eprint/23791

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