Plant Physiology 59:1128-1132 (1977)
© 1977 American Society of Plant Biologists
Articles
Enzymes of the Glycolytic and Pentose Phosphate Pathways in Proplastids from the Developing Endosperm of Ricinus communis L. 1
P. David Simcox,
E. Ellen Reid,
David T. Canvin and
David T. Dennis
a Department of Biology, Queen's University, Kingston, Ontario, Canada, K7L 3N6
The metabolism of sucrose to long chain fatty acids in the endosperm of developing castor bean (Ricinus communis L.) seeds requires a combination of cytosolic and proplastid enzymes. The total activity and the subcellular distribution of the intermediate enzymic steps responsible for the conversion of sucrose to pyruvate have been determined. Hexose phosphate synthesis from sucrose occurs in the cytosol along with the first oxidative step in the pentose phosphate pathway, glucose-6-phosphate dehydrogenase. The proplastids contain the necessary complement of glycolytic enzymes to account for the in vivo rates of acetate synthesis from glucose 6-phosphate. These organelles also contain the majority of the cellular 6-phosphogluconate dehydrogenase, transketolase, and transaldolase activities.
The consequence of these enzyme distributions is that glucose 6-phosphate or 6-phosphogluconate produced in the cytosol must be transported into the proplastids where conversion to pyruvate occurs. The unique segregation of the two oxidative steps in the pentose phosphate pathway may be required to meet the metabolic needs of these fat-storing seeds. Compartmentation of glucose-6-phosphate dehydrogenase in the cytosol and 6-phosphogluconate dehydrogenase in the proplastids is discussed in light of the NADPH requirements for fatty acid synthesis in these subcellular locations.
1 Supported by grants to D. T. C. and D. T. D. from the National Research Council of Canada.
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