Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Genetic determination of the constitutive biosynthesis of phospho-glucosidase A in Escherichia coli K-12.

Prasad I., Young B., Schaefler S.

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

J. Bacteriol. 114:909-915(1973) [PubMed] [Europe PMC]

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again