Nambiar, PT Chandrasekharan and Shethna, YI (1976) Purification and properties of an NADP+-specific isocitrate dehydrogenase from Rhizobium meliloti. [['eprint_typename_journalp' not defined]]
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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: | ['eprint_typename_journalp' not defined] |
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Additional Information: | Copyright for this article belongs to Springer. |
Subjects: | Division of Biological Sciences > Microbiology & Cell Biology |
Depositing User: | Users 849 not found. |
Date Deposited: | 20 Jan 2010 10:08 |
Last Modified: | 19 Sep 2010 05:50 |
URI: | http://eprints.iisc.ac.in/id/eprint/24400 |