Biosynthesis of isoleucine and valine in mycobacterium tuberculosis H37Rv*1: II. Purification and properties of acetohydroxy acid isomerase

Allaudeen, HS and Ramakrishnan, T (1970) Biosynthesis of isoleucine and valine in mycobacterium tuberculosis H37Rv*1: II. Purification and properties of acetohydroxy acid isomerase. In: Archives of Biochemistry and Biophysics, 140 (1). 245-&.

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Abstract

Acetohydroxy acid isomerase (AHA isomerase) was purified about 110-fold and separated from reductase and acetohydroxy acid isomeroreductase. The AHA isomerase was found to be homogeneous by agar and polyacrylamide gel electrophoreses at different pHs. The properties of AHA isomerase have been studied. The purified enzyme showed requirement for Image -ascorbic acid and sulfate ions for its activity. Synthetic ascorbic acid sulfate could replace Image -ascorbic acid and sulfate. α-Methyllactate and α-ketoisovalerate were found to inhibit AHA isomerase activity competitively whereas Image -valine and Image -isoleucine had no significant inhibitory effect. p-Hydroxymercuribenzoate inhibited AHA isomerase activity and the inhibition was reversed by β-mercaptoethanol.

Item Type:	Journal Article
Publication:	Archives of Biochemistry and Biophysics
Publisher:	Elsevier Inc
Additional Information:	Copyright of this article belongs to Elsevier Inc.
Department/Centre:	Division of Biological Sciences > Microbiology & Cell Biology
Date Deposited:	03 Jun 2010 07:37
Last Modified:	29 Jun 2011 06:47
URI:	http://eprints.iisc.ac.in/id/eprint/27930

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