Membrane Topology of Aspartate: Alanine Antiporter AspT from Comamonas testosterone

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Topology of AspT, the aspartate:alanine antiporter of Tetragenococcus halophilus, determined by site-directed fluorescence labeling.

The gram-positive lactic acid bacterium Tetragenococcus halophilus catalyzes the decarboxylation of L-aspartate (Asp) with release of L-alanine (Ala) and CO(2). The decarboxylation reaction consists of two steps: electrogenic exchange of Asp for Ala catalyzed by an aspartate:alanine antiporter (AspT) and intracellular decarboxylation of the transported Asp catalyzed by an L-aspartate-beta-decar...

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Plasmid-encoded asp operon confers a proton motive metabolic cycle catalyzed by an aspartate-alanine exchange reaction.

Tetragenococcus halophila D10 catalyzes the decarboxylation of L-aspartate with nearly stoichiometric release of L-alanine and CO(2). This trait is encoded on a 25-kb plasmid, pD1. We found in this plasmid a putative asp operon consisting of two genes, which we designated aspD and aspT, encoding an L-aspartate-beta-decarboxylase (AspD) and an aspartate-alanine antiporter (AspT), respectively, a...

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Structural and functional importance of transmembrane domain 3 (TM3) in the aspartate:alanine antiporter AspT: topology and function of the residues of TM3 and oligomerization of AspT.

AspT, the aspartate:alanine antiporter of Tetragenococcus halophilus, a membrane protein of 543 amino acids with 10 putative transmembrane (TM) helices, is the prototype of the aspartate:alanine exchanger (AAE) family of transporters. Because TM3 (isoleucine 64 to methionine 85) has many amino acid residues that are conserved among members of the AAE family and because TM3 contains two charged ...

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Membrane topology of the metal-tetracycline/H+ antiporter TetA(K) from Staphylococcus aureus.

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Electrogenic characteristics of the mitochondrial glutamate-aspartate antiporter.

Rat liver mitochondria were loaded with aspartate by treating glutamate-loaded mitochondria with oxalacetate. Aspartate e&x was initiated by addition of extramitochondrial glutamate and was accompanied by the uptake of an equivalent amount of glutamate and protons. Proton uptake, however, did not occur in the presence of an uncoupling agent, and net transport of aspartate was facilitated by the...

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ژورنال

عنوان ژورنال: The Journal of Biochemistry

سال: 2007

ISSN: 1756-2651,0021-924X

DOI: 10.1093/jb/mvm079