Literature DB >> 239745

Regulation of glucose-6-phosphate dehydrogenase in spinach chloroplasts by ribulose 1,5-diphosphate and NADPH/NADP+ ratios.

K Lendzian, J A Bassham.   

Abstract

The activity of glucose-6-phosphate dehydrogenase (EC 1.1.1.49) FROM SPINACH CHLOROPLASTS IS STRONGLY REGULATED BY THE RATIO OF NADPH/NADP+, with the extent of this regulation controlled by the concentration of ribulose 1,5-diphosphate. Other metabolites of the reductive pentose phosphate cycle are far less effective in mediating the regulation of the enzyme activity by NADPH/NADP+ ratio. With a ratio of NADPH/NADP+ of 2, and a concentration of ribulose 1,5-diphosphate of 0.6 mM, the activity of the enzyme is completely inhibited. This level of ribulose 1,5-diphosphate is well within the concentration range which has been reported for unicellular green algae photosynthesizing in vivo. Ratios of NADPH/NADP+ of 2.0 have been measured for isolated spinach chloroplasts in the light and under physiological conditions. Since ribulose 1,5-diphosphate is a metabolite unique to the reductive pentose phosphate cycle and inhibits glucose-6-phosphate dehydrogenase in the presence of NADPH/NADP+ ratios found in chloroplasts in the light, it is proposed that regulation of the oxidative pentose phosphate cycle is accomplished in vivo by the levels of ribulose 1,5-diphosphate, NADPH, and NADP+. It already has been shown that several key reactions of the reductive pentose phosphate cycle in chloroplasts are regulated by levels of NADPH/NADP+ or other electron-carrying cofactors, and at least one key-regulated step, the carboxylation reaction is strongly affected by 6-phosphogluconate, the metabolic unique to the oxidative pentose phosphate cycle. Thus there is an interesting inverse regulation system in chloroplasts, in which reduced/oxidized coenzymes provide a general regulatory mechanism. The reductive cycle is activated at high NADPH/NADP+ ratios where the oxidative cycle is inhibited, and ribulose 1,5-diphosphate and 6-phosphogluconate provide further control of the cycles, each regulating the cycle in which it is not a metabolite.

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Year:  1975        PMID: 239745     DOI: 10.1016/0005-2728(75)90040-7

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  32 in total

1.  Light modulation of glucose-6-phosphate dehydrogenase: partial characterization of the light inactivation system and its effects on the properties of the chloroplastic and cytoplasmic forms of the enzyme.

Authors:  L E Anderson; J X Duggan
Journal:  Plant Physiol       Date:  1976-08       Impact factor: 8.340

2.  Interaction between Chloroplasts and Mitochondria in Microalgae: Role of Glycolysis.

Authors:  F Rebeille; P Gans
Journal:  Plant Physiol       Date:  1988-12       Impact factor: 8.340

3.  A possible plasma membrane particle containing malic enzyme activity.

Authors:  P Pupillo; E Del Grosso
Journal:  Planta       Date:  1981-05       Impact factor: 4.116

4.  Carbon metabolism of chloroplasts in the dark: Oxidative pentose phosphate cycle versus glycolytic pathway.

Authors:  W M Kaiser; J A Bassham
Journal:  Planta       Date:  1979-01       Impact factor: 4.116

5.  Activation of ribulose-1,5-bisphosphate carboxylase by chloroplast metabolites in a reconstituted spinach chloroplast system.

Authors:  K J Lendzian
Journal:  Planta       Date:  1978-01       Impact factor: 4.116

6.  Properties and physiological function of a glutathione reductase purified from spinach leaves by affinity chromatography.

Authors:  B Halliwell; C H Foyer
Journal:  Planta       Date:  1978-01       Impact factor: 4.116

7.  Interactions between magnesium ions, pH, glucose-6-phosphate, and NADPH/NADP(+) ratios in the modulation of chloroplast glucose-6-phosphate dehydrogenase in vitro.

Authors:  K J Lendzian
Journal:  Planta       Date:  1978-01       Impact factor: 4.116

8.  Chloroplast glutathione reductase.

Authors:  M Schaedle
Journal:  Plant Physiol       Date:  1977-05       Impact factor: 8.340

9.  Differential regulation of glucose-6-phosphate dehydrogenase isoenzyme activities in potato.

Authors:  Rüdiger Hauschild; Antje von Schaewen
Journal:  Plant Physiol       Date:  2003-09       Impact factor: 8.340

10.  In Vivo and in Vitro Studies of Glucose-6-Phosphate Dehydrogenase from Barley Root Plastids in Relation to Reductant Supply for NO2- Assimilation.

Authors:  D. P. Wright; H. C. Huppe; D. H. Turpin
Journal:  Plant Physiol       Date:  1997-08       Impact factor: 8.340

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