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In Lactobacillus bulgaricus the genes coding for phosphofructokinase and pyruvate kinase are clustered into one operon, although the reactions catalyzed by these two enzymes are seven steps apart along glycolysis. The translation of the unique messenger RNA should yield equi- valent amounts of these two proteins, but their allosteric properties allow an independent control of the levels of their enzymatic activities. This enzymatic regulation involves a 'Ioop' in which the substrate of one enzyme is an allosteric effector of the other: fructose-6-phosphate, the sub- strate of phosphofructokinase, is an activator of pyruvate kinase, and phospho-enol-pyruvate, the substrate of pyruvate kinase, is an inhibitor of phosphofructokinase. Such a metabolic control, with an ante-activation by fructose-6-phosphate and a feed-back inhibition by phospho-enol- pyruvate, contributes to the damping of changes in the glycolytic flux. In L. bulgaricus, the two key enzymes phosphofructokinase and pyruvate kinase are therefore coupled at the level ofboth their coordinated biosynthesis and the mutual control of their activities, which suggests that they are indeed involved in regulating the yield of D-lactate in fermentation. © Inra/Elsevier, Paris. Lactobacillus bulgaricus / glycolysis / allosteric regulation / phosphofructokinase / pyruvate kinase

Enzymatic and genetic régulation of glycolysis in Lactobacillus delbrueckii subsp. bulgaricus