The subcellular location and characteristics of pyrophosphate-fructose-6-phosphate 1-phosphotransferase from suspension-cultured cells of soybean |
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| Authors: | F D Macdonald J Preiss |
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| Institution: | (1) Department of Biochemistry and Biophysics, University of California, 95616 Davis, CA, USA;(2) Present address: Division of Molecular Plant Biology, University of California, Hilgard Hall, 94720 Berkeley, CA, USA;(3) Present address: Biochemistry Department, Michigan State University, 48824 East Lansing, MI, USA |
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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.Abbreviations PFP
pyrophosphate-fructose-6-phosphate 1-phosphotransferase
- Pi
phosphate
- PPi
pyrophosphate |
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| Keywords: | Cell culture (enzyme localization) Glycine (enzyme localization) Pyrophosphate-fructose-6-phosphate 1-phosphotransferase |
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