Abstract
Gest and Mandelstam have reported1 that β-galactosidase from Escherichia coli is more heat labile in the presence of fructose-1,6-diphosphate (FDP) than in its absence. They found the effect to be quite specific: of the other sugars and phosphorylated esters tested, only glucose-6-phosphate (G6P) weakly, but significantly, increased the heat lability of the enzyme. These results support the possibility that β-galactosidase possesses a specific binding site for FDP. Gest and Mandelstam1 suggested that FDP, which is a key intermediate in carbohydrate metabolism, might be the repressor metabolite postulated by Vogel2 and Szilard3. If this were true, catabolite repression would be effected by the production of FDP, which would then combine with nascent β-galactosidase to prevent the enzyme from leaving the ribosomes on which it is being synthesized.
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References
Gest, H., and Mandelstam, J., Nature, 211, 72 (1966).
Vogel, H. J., Proc. U.S. Nat. Acad. Sci., 43, 491 (1957).
Szilard, L., Proc. U.S. Nat. Acad. Sci., 46, 271 (1960).
Prevost, C., and Moses, V., Biochem. J. (in the press).
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Jacob, F., and Monod, J., J. Mol. Biol., 3, 318 (1961).
Palmer, J., and Moses, V., Biochem. J. (in the press).
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BREWER, M., MOSES, V. Metabolite-promoted Heat Lability of β-Galactosidase and its Relation to Catabolite Repression. Nature 214, 272–273 (1967). https://doi.org/10.1038/214272a0
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DOI: https://doi.org/10.1038/214272a0
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