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The subcellular location and characteristics of pyrophosphate-fructose-6-phosphate 1-phosphotransferase from suspension-cultured cells of soybean

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Abstract

The cytoplasm was identified as the probable location of pyrophosphate-fructose-6-phosphate 1-phosphotransferase (EC 2.7.1.90) in suspension-cultured cells of soybean (Glycine max L.). The characteristics of the partially purified enzyme were investigated. The activity was strongly dependent on the presence of fructose 2,6-bisphosphate and this activator exerted its effects through a dramatic increase in the affinity of the enzyme for its substrates, fructose 6-phosphate and inorganic pyrophosphate. Saturation curves for all substrates were hyperbolic. The apparent molecular weight of the partially purified enzyme was 183000 by gel filtration chromatography and 128000 by sucrose-density-gradient centrifugation. The activation by fructose 2,6-bisphosphate was not accompanied by any measurable change in molecular weight. The possible role of this enzyme in the metabolism of non-photosynthetic sink tissues is discussed.

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Abbreviations

PFP:

pyrophosphate-fructose-6-phosphate 1-phosphotransferase

Pi :

phosphate

PPi :

pyrophosphate

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Author notes

  1. F. D. Macdonald

    Present address: Division of Molecular Plant Biology, University of California, Hilgard Hall, 94720, Berkeley, CA, USA

  2. J. Preiss

    Present address: Biochemistry Department, Michigan State University, 48824, East Lansing, MI, USA

Authors and Affiliations

  1. Department of Biochemistry and Biophysics, University of California, 95616, Davis, CA, USA

    F. D. Macdonald & J. Preiss

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  1. F. D. Macdonald
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  2. J. Preiss
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Macdonald, F.D., Preiss, J. The subcellular location and characteristics of pyrophosphate-fructose-6-phosphate 1-phosphotransferase from suspension-cultured cells of soybean. Planta 167, 240–245 (1986). https://doi.org/10.1007/BF00391421

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  • DOI: https://doi.org/10.1007/BF00391421

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