Exchange of glutamate and gamma-aminobutyrate in a Lactobacillus strain

J Bacteriol. 1997 May;179(10):3362-4. doi: 10.1128/jb.179.10.3362-3364.1997.

Abstract

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.

MeSH terms

  • Adenosine Triphosphate / antagonists & inhibitors
  • Adenosine Triphosphate / biosynthesis
  • Biological Transport
  • Carbon Dioxide / metabolism
  • Decarboxylation
  • Dicyclohexylcarbodiimide / pharmacology
  • Glutamic Acid / metabolism*
  • Lactobacillus / metabolism*
  • Proton-Motive Force
  • Proton-Translocating ATPases / antagonists & inhibitors
  • gamma-Aminobutyric Acid / metabolism*

Substances

  • Carbon Dioxide
  • Glutamic Acid
  • Dicyclohexylcarbodiimide
  • gamma-Aminobutyric Acid
  • Adenosine Triphosphate
  • Proton-Translocating ATPases