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J. Bacteriol., 05 1997, 3362-3364, Vol 179, No. 10
Copyright © 1997, American Society for Microbiology

Exchange of glutamate and gamma-aminobutyrate in a Lactobacillus strain

T Higuchi, H Hayashi and K Abe
Soy Sauce Research Laboratory, R & D Division of Kikkoman Corporation, Noda City, Chiba, Japan. LDY05507@niftyserve.or.jp

Lactobacillus sp. strain E1 catalyzed the decarboxylation of glutamate (Glu), resulting in a nearly stoichiometric release of the products gamma-aminobutyrate (GABA) and CO2. This decarboxylation was associated with the net synthesis of ATP. ATP synthesis was inhibited almost completely by nigericin and about 70% by N,N'-dicyclohexylcarbodiimide (DCCD), without inhibition of the decarboxylation. These findings are consistent with the possibility that a proton motive force arises from the cytoplasmic proton consumption that accompanies glutamate decarboxylation and the electrogenic Glu/GABA antiporter and the possibility that this proton motive force is coupled with ATP synthesis by DCCD-sensitive ATPase.


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