Purification and properties of protocatechuate-3,4-dioxygenase from Tecoma stans L

Mohan, VP and Kishore, G and Sugumaran, M and Vaidyanathan, CS (1979) Purification and properties of protocatechuate-3,4-dioxygenase from Tecoma stans L. In: Plant Science Letters, 16 (2-3). 267 -272.

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Abstract

Protocatechuate-3,4-dioxygenase from the leaves of Tecoma stans was purified to near homogeneity and some of its properties studied. It was optimally active at pH 5.2 and at 40°C. Its molecular weight of approx. 150 000 was determined by gel filtration on a Sephadex G-150 column. The Km value for protocatechuate was found to be 330 μM and for ferrous sulfate, 40 μM. The enzyme was highly specific for protocatechuate and did not attack any of the substrate analogues. None of the substrate analogues tested inhibited the enzyme activity. Sulfhydryl reagents inhibited the enzyme activity which could be partially reversed by sulfhydryl compounds. The dioxygenase activity was not associated with polyphenol oxidase activity.

Item Type:	Journal Article
Publication:	Plant Science Letters
Publisher:	Elsevier Science
Additional Information:	Copy right of this article belongs to Elsevier Science.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	05 Jan 2010 05:51
Last Modified:	19 Sep 2010 05:52
URI:	http://eprints.iisc.ac.in/id/eprint/24854

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