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J Bacteriol. 1967 March; 93(3): 1009-1016
Copyright © 1967 American Society for Microbiology. All Rights Reserved.

Properties of the Glutamate Transport System in Escherichia coli

Yeheskel S. Halpern and Avivith Even-Shoshan

Department of Bacteriology, Hebrew University-Hadassah Medical School, Jerusalem, Israel

ABSTRACT

The properties of the glutamate transport system in two glutamate-utilizing mutants of Escherichia coli K-12 were investigated. Growth in the presence of glutamate enhanced the capacity of the bacteria for glutamate uptake. Accumulation of glutamate was found to be an energy-linked highly temperature-dependent process. Nonlinear double reciprocal plots of uptake were obtained in the absence of an exogenous energy source and in the presence of glucose or glycerol. Addition of {gamma}-aminobutyrate, succinate, ketoglutarate, or aspartate accelerated glutamate uptake and brought about "normalization" of its kinetics. Straight-line kinetics of uptake was also observed when succinate served as the source of energy. Under these conditions, aspartate and {alpha}-ketoglutarate inhibited glutamate uptake in a noncompetitive fashion, whereas {gamma}-aminobutyrate activated the system. A number of other amino acids were found to act as "noncompetitive" inhibitors. D-glutamate and some derivatives of glutamate with an unsubstituted {alpha}-carboxylic and {alpha}-amino group inhibited L-glutamate uptake in a strictly competitive fashion. An allosteric permease model, consistent with all of these findings, is proposed.

J Bacteriol. 1967 March; 93(3): 1009-1016
Copyright © 1967 American Society for Microbiology. All Rights Reserved.





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