Isophenoxazine synthase

Nair, Madhusudanan P and Vaidyanathan, CS (1964) Isophenoxazine synthase. In: Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 81 (3). pp. 507-516.

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Abstract

An enzyme which catalyses the oxidation of o-aminophenol to o-quinoneimine and the subsequent condensation of o-aminophenol and o-quinoneime to give isophenoxazine has been isolated from the leaves of Tecoma stans. The reaction had an optimum pH of 6.2 and an optimum temperature of 45°. Heavy-metal ions like Hg2+, Co2+, Mg2+, Fe3+, were inhibitory. Mn2+ activated the reaction to about 40%. The reaction requires intact sulfhydryl groups. A study of the coenzyme requirements showed that isophenoxazine synthase (o-aminophenol: O2 oxidoreductase) is a flavoprotein requiring FAD for maximum activity. Stoichiometric studies showed that 2 moles of o-aminophenol gave 1 mole of isophhenoxazine.

Item Type:	Journal Article
Publication:	Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	24 May 2010 07:23
Last Modified:	19 Sep 2010 06:07
URI:	http://eprints.iisc.ac.in/id/eprint/28085

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