Regulation of glycolysis by adenosine diphosphate in Pisum sativum |
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Authors: | Curtis V. Givan |
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Affiliation: | Department of Plant Biology, University of Newcastle upon Tyne, Newcastle upon Tyne, NE1 7RU, England |
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Abstract: | The role of ADP in controlling glycolysis has been examined in a soluble extract of germinating pea seeds. A shortage of ADP appears to retard glycolysis principally by restricting the conversion of phosphopyruvate to pyruvate rather than by restricting formation of phosphoglycerate. Upon addition of ADP to the extract there is an immediate decrease in the concentration of phosphopyruvate accompanied by an increase in pyruvate. Apparently the pyruvate-kinase step shows the most marked response to fluctuations in ADP availability. The glycolytic response to ADP depends on the concentration of ATP magnesium ions. The relation of magnesium-ion availability to adenine-nucleotide control of glycolysis is discussed. |
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Keywords: | Leguminosae glycolysis fermentation metabolic regulation adenine nucleotides pyruvate kinase. ADP, adenosine diphosphate ATP, adenosine triphosphate PFK, phosphofructokinase PK, pyruvate kinase CAP, glyceraldehyde-P DHAP, dihydroxyacetone-P 3-PGA, 3-phosphoglycerate 2-PGA, 2-phosphoglycerate 1,3-di-PGA, 1,3-diphosphoglycerate FDP, fructose diphosphate G6P, glucose 6-P F6P, fructose 6-P. |
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