| Literature DB >> 6793015 |
Abstract
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, Mg2+-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 (alpha-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.Entities:
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Year: 1981 PMID: 6793015 DOI: 10.1007/BF00406456
Source DB: PubMed Journal: Arch Microbiol ISSN: 0302-8933 Impact factor: 2.552