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Genetic Determination of the Constitutive Biosynthesis of Phospho-ß-Glucosidase A in Escherichia coli K-12

¹ The Public Health Research Institute of the City of New York, Inc., and Department of Health, Bureau of Laboratories, New York, New York 10016

ABSTRACT

Escherichia coli wild-type cells form constitutively the enzyme phospho-ß-glucosidase A, which has a high affinity for phosphorylated aromatic ß-glucosides and a low affinity for phosphorylated ß-methyl-glucoside. Phospho-ß-glucosidase B and ß-glucoside permease I are formed in aromatic ß-glucoside-fermenting mutants. Mutants lacking phospho-ß-glucosidases A and B have been isolated. These mutants showed a reduced rate of inducibility of the ß-glucoside permease I. The restoration of phospho-ß-glucosidase A or B activity resulted in an increased rate of induction of the ß-glucoside permease I. The presence of the phospho-ß-glucosidases was not required for the constitutive biosynthesis of the ß-glucoside permease. Mutants selected for growth on ß-methyl-glucoside as carbon source showed an increased level of constitutive phospho-ß-glucosidase A activity. Gene bglD, the structural gene for phospho-ß-glucosidase A, was mapped between the pyrE locus and the cluster bgl loci, whereas bglE, the regulatory site determining the hyperproduction of phospho-ß-glucosidase A, was mapped between the bgl and ilv clusters. The bglE locus appears to have a regulatory effect on the expression of the bglD gene.

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