TY - JOUR
T1 - Exchange of glutamate and γ-aminobutyrate in a Lactobacillus strain
AU - Higuchi, Takeshi
AU - Hayashi, Hisanobu
AU - Abe, Keietsu
PY - 1997/5
Y1 - 1997/5
N2 - Lactobacillus sp. strain E1 catalyzed the decarboxylation of glutamate (Glu), resulting in a nearly stoichiometric release of the products γ- 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.
AB - Lactobacillus sp. strain E1 catalyzed the decarboxylation of glutamate (Glu), resulting in a nearly stoichiometric release of the products γ- 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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U2 - 10.1128/jb.179.10.3362-3364.1997
DO - 10.1128/jb.179.10.3362-3364.1997
M3 - Article
C2 - 9150237
AN - SCOPUS:0030977050
SN - 0021-9193
VL - 179
SP - 3362
EP - 3364
JO - Journal of Bacteriology
JF - Journal of Bacteriology
IS - 10
ER -