1989
DOI: 10.1128/jb.171.2.1118-1125.1989
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Mechanism of L-glutamate transport in membrane vesicles from Bacillus stearothermophilus

Abstract: In the presence of electrochemhical energy, several branched-chain neutral and acidic amino acids were found to accumulate in membrane vesicles of Bacillus stearothermophilus. The membrane vesicles contained a stereo-specific transport system for the acidic amino acids L-glutamate and L-aspartate, which could not translocate their respective amines, L-glutamihe and L-asparagine. The transport system was thermostable (T1 = 700C) and showed highest activities at elevated temperatures (60 to 65°C). The

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Cited by 43 publications
(36 citation statements)
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“…The transport by the GItT proteins is driven by the proton motive force (Ap) and also by inwardly directed Na ÷ gradients (~pNa), and transport of L-glutamate probably occurs in symport with one H ÷ and one Na ÷ (De Vrij et aL, 1989;Heyne et aL, 1991). A similar type of Na÷-H+-glutamate symport has been found in the thermophile Bacillus IS1 (GItTBi) (B.…”
mentioning
confidence: 86%
“…The transport by the GItT proteins is driven by the proton motive force (Ap) and also by inwardly directed Na ÷ gradients (~pNa), and transport of L-glutamate probably occurs in symport with one H ÷ and one Na ÷ (De Vrij et aL, 1989;Heyne et aL, 1991). A similar type of Na÷-H+-glutamate symport has been found in the thermophile Bacillus IS1 (GItTBi) (B.…”
mentioning
confidence: 86%
“…In Lactococcus lactis the symport systems studied so far use protons as coupling ion [8,39]. For Bacillus stearothermophilus electrogenic uptake of glutamate with a proton plus sodium ion has been described [26,55]. Sodium ion is the predominant cation for solute transport in the examined alkaliphilic, halophilic, thermophilic and marine bacteria.…”
Section: Ii-c Electrogenic Solute-cation Symport (mentioning
confidence: 99%
“…Serine uptake was also inhibited when high internal Na+ concentrations were employed (data not shown). In the thermophilic aerobic bacterium B. stearothermophilus, glutamate is taken up in symport with 1 H+ and 1 Na+ (6). Such a Na+/H+/glutamate symport system was also reported for E. coli (9), but recently two distinct genes encoding two different secondary transport proteins were cloned (4).…”
Section: Discussionmentioning
confidence: 99%
“…Secondary transport systems in this * Corresponding author. organism are Na+ symport systems, except for glutamate, which is symported together with a H+ and Na+ ion, and lysine, which is transported via a uniport mechanism (6,18). For anaerobic thermophilic bacteria, which derive relatively little metabolic energy from their substrates and produce ApH dissipating fatty acids, the mechanism of energy-transducing processes is not well established but may very well differ from that in the aerobes.…”
mentioning
confidence: 99%