Allosteric inhibition by phosphoenolpyruvate of glucose-6-phosphate dehydrogenase from bacteria and its taxonomic importance |
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| Authors: | R. Opitz H.G. Schlegel |
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| Affiliation: | 1. Institut für Mikrobiologie der Gesellschaft für Strahlen und Umweltforschung mbH München, West Germany;2. Institut für Mikrobiologie der Universität, Grisebachstr. 8,3400 Göttingen, West Germany |
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| Abstract: | Purified glucose-6-phosphate dehydrogenase from Zymomonas mobilis was examined with respect to inhibition by phosphoenolpyruvate, ADP and ATP. Its molecular weight was 260,000 and the kinetics of substrate conversion indicated a random bi bi mechanism. This enzyme and the dehydrogenases from Z. anaerobia, Azotobacter chroococcum, A. vinelandii, and “Corynebacterium” autotrophicum strain 19/-/x were found to be allosterically inhibited by phosphoenolpyruvate, while those from several coryneform bacteria and from Escherichia coli or Pseudomonas fluorescens were not. |
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| Keywords: | Glucose-6-phosphate dehydrogenase phosphoenolpyruvate ATP allosteric inhibition Zymomonas Azotobacter identification of genera |
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