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Inhibition of mevalonate kinase by disulfide compounds

Lalitha, R and Kalpana, GV and Ramasarma, T (1986) Inhibition of mevalonate kinase by disulfide compounds. In: Indian Journal of Biochemistry & Biophysics, 23 (4). pp. 204-207.

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Abstract

Mevalonate kinase (I) of rat liver could use ADP in place of ATP at low, nonsaturated concentrations of mevalonate. I was inhibited when both dithiothreitol (DTT) and $Fe^{2+}$ (or $Fe^{3+})$ were added, and this inhibitory effect was obtained in Tris, but not in phosphate buffer. The inhibition appeared to be specific for DTT among the thiols tested. Since DTT was known to be oxidized by $Fe^{2+}$ in Tris, but not in phosphate buffer, the above inhibition was found to be a response to disulfide compounds of which cystamine was the most effective. A similar effect of DTT and $Fe^{2+}$ was, however, not obtained for I from a plant source (lemongrass leaves) although the addition of DTT was essential for activity. These findings add I to the growing list of enzymes whose activity is regulated by thiol-disulfide exchange reaction.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Council of Scientific & Industrial Research.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 30 May 2008
Last Modified: 27 Aug 2008 13:22
URI: http://eprints.iisc.ernet.in/id/eprint/13972

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