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  • Title: Glutamate transport in membrane vesicles of the wild-type strain and glutamate-utilizing mutants of Escherichia coli.
    Author: Kahane S, Marcus M, Metzer E, Halpern YS.
    Journal: J Bacteriol; 1976 Mar; 125(3):770-5. PubMed ID: 767326.
    Abstract:
    A highly specific energy-dependent glutamate transport system was demonstrated in membrane vesicles of glutamate-utilizing Escherichia coli K-12 mutants. The glutamate transport activity of membranes from the parent strain, unable to grow on glutamate, was very low. With ascorbate-phenazine methosulfate as the electron donor, mutant preparations displayed 17 to 20 times higher activity than did the wild type. However, the affinity of the mutant carrier for L-glutamate remained the same as in the parent strain. Comparative inhibition analysis of glutamate transport in whole cells and membrane vesicles and of in vitro binding of glutamate to a specific periplasmic-binding protein suggests that under certain conditions the latter may be a component of the E. coli K-12 glutamate transport system.
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