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Regulation of glucose 6 phosphate dehydrogenase in brevibacterium flavum


, : Regulation of glucose 6 phosphate dehydrogenase in brevibacterium flavum. Agricultural & Biological Chemistry 51(1): 101-108

NADP-Specific G6P dehydrogenase was partially purified from Brevibacterium flavum. Its activity, with an optimum pH of 7.5, was stabilized by KCl or Mg2+ and inhibited by diamide, a sulfhydryl reagent. It was also inhibited by oxaloacetate, FBP, PRPP, acetyl-CoA, Ru5P, xylulose 5-phosphate and NADPH. Among them, oxaloacetate showed the strongest inhibition. The concentration of oxaloacetate giving 50% inhibition was 0.09 mM. The inhibitions by oxaloacetate, FBP, PRPP, and NADPH were non-competitive, mixed, and competitive for both the substrates, respectively. Oxaloacetate in combination with FBP, PRPP, or Ru5P inhibited the activity cumulatively. The sensitivities to the oxaloacetate, FBP, and PRPP inhibitions were lost on ammonium sulfate treatment, whereas that to NADPH inhibition was not affected at all. The inhibition by oxaloacetate was specific to glutamate-producing bacteria belonging to the genera, Brevibacterium and Corynebacterium, in contrast to those by FBP and PRPP, which were found in almost all bacteria tested. G6P dehydrogenase in B. flavum was induced by glucose when it was cultured on acetate, succinate, or glutamate.

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Shiio, I.; Ozaki, H., 1970: Regulation of nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase from Brevibacterium flavum, a glutamate-producing bacterium. Journal of Biochemistry 68(5): 633-647

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