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Metabolic regulation of the glucose-6-phosphate dehydrogenase from Paracoccus denitrificans grown on glucose/nitrate

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Abstract

Glucose-6-phosphate dehydrogenase (d-glucose-6-phosphate: NADP+ l-oxidoreductase EC 1.1.1.49) isolated from Paracoccus denitrificans grown on glucose/nitrate exhibits both NAD+-and NADP+-linked activities. Both activities have a pH optimum of pH 9.6 (Glycine/NaOH buffer) and neither demonstrates a Mg2+ requirement. Kinetics for both NAD(P)+ and glucose-6-phosphate were investigated. Phosphoenolpyruvate inhibits both activities in a competitive manner with respect to glucose-6-phosphate. ATP inhibits the NAD+-linked activity competitively with respect to glucose-6-phosphate but has no effect on the NADP+-linked activity. Neither of the two activities are inhibited by 100 μM NADH but both are inhibited by NADPH. The NAD+-linked activity is far more sensitive to inhibition by NADPH than the NADP+-linked activity.

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Correspondence to A. R. Slabas.

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Slabas, A.R., Wahtley, F.R. Metabolic regulation of the glucose-6-phosphate dehydrogenase from Paracoccus denitrificans grown on glucose/nitrate. Arch. Microbiol. 112, 225–227 (1977). https://doi.org/10.1007/BF00429339

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Key words

  • Glucose-6-phosphate dehydrogenase
  • Paracoccus denitrificans
  • Nicotinamide adenine dinucleotide (phosphate)
  • Adenosinetriphosphate
  • Phosphoenolpyruvate
  • Enzyme regulation