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Purification and properties of an NADP+-specific isocitrate dehydrogenase from Rhizobium meliloti

Nambiar, PT Chandrasekharan and Shethna, YI (1976) Purification and properties of an NADP+-specific isocitrate dehydrogenase from Rhizobium meliloti. In: Antonie van Leeuwenhoek, 42 (4). pp. 471-482.

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Abstract

An NADP+-specific isocitrate dehydrogenase has been purified and characterized from Rhizobium meliloti. The enzyme showed Mn++ or Mg++ requirement. The apparent Km values were 2.00×10-5 m and 1.51×10-5 m for dl-isocitrate and NADP+, respectively. The enzyme was inhibited by ATP, to a lesser extent by ADP and AMP. agr-Ketoglutarate also inhibited the enzyme activity. Oxalacetate and glyoxylate together inhibited the enzyme activity. The inhibition was competitive. Studies with thiol inhibitors suggested that the enzyme contained a sulfhydryl group at or near the active site. The enzyme has an approximate molecular weight of 60 000. Fluorescence studies suggested that the enzyme contained tryptophan.

Item Type: Journal Article
Additional Information: Copyright for this article belongs to Springer.
Department/Centre: Division of Biological Sciences > Microbiology & Cell Biology
Date Deposited: 20 Jan 2010 10:08
Last Modified: 19 Sep 2010 05:50
URI: http://eprints.iisc.ernet.in/id/eprint/24400

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