Exchange of glutamate and gamma-aminobutyrate in a Lactobacillus strain.
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.
Higuchi
T
T
Soy Sauce Research Laboratory, R & D Division of Kikkoman Corporation, Noda City, Chiba, Japan. LDY05507@niftyserve.or.jp
Hayashi
H
H
Abe
K
K
D000255:Adenosine Triphosphate / Q000037:antagonists & inhibitors / Q000096:biosynthesis; D001692:Biological Transport; D002245:Carbon Dioxide / Q000378:metabolism; D003653:Decarboxylation; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D018698:Glutamic Acid / Q000378:metabolism*; D007778:Lactobacillus / Q000378:metabolism*; D018892:Proton-Motive Force; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors; D005680:gamma-Aminobutyric Acid / Q000378:metabolism*
D002245:Carbon Dioxide; D018698:Glutamic Acid; D004024:Dicyclohexylcarbodiimide; D005680:gamma-Aminobutyric Acid; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases