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

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...

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Bibliographic Details
Published in:Planta 1986-02, Vol.167 (2), p.240-245
Main Authors: Macdonald, F.D, Preiss, J
Format: Article
Language:English
Subjects:
Biological and medical sciences
Cell biochemistry
Cell physiology
cell suspension culture
Cytoplasm
Dehydrogenases
Diphosphates
Enzymes
Fundamental and applied biological sciences. Psychology
Glycine max
Kinetics
Molecular weight
Phosphates
Plant physiology and development
Protoplasts
Soybeans
Starches
transferases
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Summary: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.
ISSN:0032-0935
1432-2048
DOI:10.1007/BF00391421