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Isolation and properties of an isocitrate dehydrogenase fromAnacystis nidulans

✍ Scribed by Gamil M. Friga; Gábor L. Farkas

Publisher
Springer
Year
1981
Tongue
English
Weight
347 KB
Volume
129
Category
Article
ISSN
0302-8933

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✦ Synopsis

A NADP+-specific isocitrate dehydrogenase (EC 1.1.1.42) was isolated and purified over 400-fold from Anacystis nidulans. The enzyme activity responded slowly to rapid changes in ligand (NADP +, isocitrate, Mg 2 +-ions) or enzyme concentration as well as to rapid changes in temperature. These are properties characteristic of the hysteretic enzymes. In addition, the enzyme activity was subject to product (c~-ketoglutarate) inhibition. ATP, ADP and CDP also inhibited the enzyme. Unlike several other cyanobacterial enzymes, the isocitrate dehydrogenase of Anacystis is not under redox control.

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