Abstract
Glutamate decarboxylase (EC 4.1.1.15) of Escherichia coli reacts with L-γ-fluoroglutamate to form α-fluoro-γ-aminobutyric acid. This reaction has been characterized, and the two fluorinated amino acids have been investigated as selective inhibitors of γ-aminobutyric acid metabolism in the nervous system. L-γ-Fluoroglutamate inhibits the glutamate decarboxylase from calf brain (Ki = 1.4 x 10-2 M) at concentrations comparable to the Km of this enzyme for glutamate (10-2 M). In addition, α-fluoro-γ-aminobutyric acid inhibits the uptake of γ-aminobutyric acid in a nerve-muscle preparatiom from lobster.
- Copyright ©, 1970, by Academic Press Inc.
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