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Enzyme-catalysed non-oxidative decarboxylation of aromatic acids: I.Purification and spectroscopic properties of 2,3 dihydroxybenzoic acid decarboxylase from Aspergillus Niger

Kamath, Ajith V and Dasgupta, Dipak and Vaidyanathan, CS (1987) Enzyme-catalysed non-oxidative decarboxylation of aromatic acids: I.Purification and spectroscopic properties of 2,3 dihydroxybenzoic acid decarboxylase from Aspergillus Niger. In: Biochemical and Biophysical Research Communications, 145 (1). pp. 586-595.

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Abstract

In order to understand the molecular mechanism of non-oxidative decarboxylation of aromatic acids observed in microbial systems, 2,3 dihydroxybenzoic acid (DHBA) decarboxylase from Aspergillus Niger was purified to homogeneity by affinity chromatography. The enzyme (Mr 120 kDa) had four identical subunits (28 kDa each) and was specific for DHBA. It had a pH optimum of 5.2 and Km was 0.34mM. The decarboxylation did not require any cofactors, nor did the enzyme had any pyruvoyl group at the active site. The carboxyl group and hydroxyl group in the Ortho-position were required for activity. The preliminary spectroscopic properties of the enzyme are also reported.

Item Type: Journal Article
Publication: Biochemical and Biophysical Research Communications
Publisher: Elsevier
Additional Information: Copyright of this article belongs to the Elsevier
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 14 May 2008
Last Modified: 19 Sep 2010 04:44
URI: http://eprints.iisc.ac.in/id/eprint/13979

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