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

✍ Scribed by P. T. Chandrasekharan Nambiar; Y. I. Shethna

Publisher
Springer Netherlands
Year
1976
Tongue
English
Weight
511 KB
Volume
42
Category
Article
ISSN
0003-6072

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✦ Synopsis

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 x 10(-5) M and 1.51 x 10(-5) M for DL-isocitrate and NADP+, respectively. The enzyme was inhibited by ATP, to a lesser extent by ADP and AMP. alpha-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.

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