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The diastereomers of -fluoroglutamate: complementary structural analogues.

The racemates of the diastereomers of γ-fluoroglutamate have been separated by ion-exchange chromatography, and the relative configuration of the 2 asymmetrical carbon atoms has been established by an unambiguous chemical method. The two diastereomers of L-γ-fluoroglutamate were prepared enzymatically, and both (on their appropriate derivatives) are substrates for the following enzymes: glutamate dehydrogenase (EC 1.4.1.3), glutamine synthetase (EC 6.3.1.2), glutamate decarboxylase (EC 4.1.1.15), carboxypeptidase G(EC 3.4.2.6), and leucine aminopeptidase (EC 3.4.1.1). The reactions of these enzymes and D-glutamate cyclase (EC 4.2.1.54) confirm the tentative assignment of configurations at the α-carbon of γ-fluoroglutamate that was proposed previously. Preliminary kinetic studies with several of these enzymes normally reactive with glutamate indicate that the threo tends to be more reactive than the erythro diastereomer. Possible biological and biochemical applications of these glutamate analogues are discussed.