Soluble and membrane-bound aspartate-binding activities in Salmonella typhimurium.
The specificities of the soluble and membrane aspartate-binding activities were compared with each other and with the specificity of aspartate chemotaxis and were found to be distinct. The soluble aspartate-binding protein was purified to homogeneity and had a molecular weight of 30,000. The dissociation constant was 10(-6) M for aspartate, and the protein bound glutamate, cysteic acid, and 2-amino-3-phosphonopropionate. Aspartate transport was inhibited by cysteic acid.
D001224:Aspartic Acid / Q000031:analogs & derivatives / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D001667:Binding, Competitive; D001693:Biological Transport, Active / Q000187:drug effects; D002462:Cell Membrane / Q000378:metabolism; D002633:Chemotaxis; D003544:Cysteic Acid / Q000378:metabolism / Q000494:pharmacology; D004229:Dithiothreitol / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D005971:Glutamates / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D011422:Propionates / Q000378:metabolism; D011955:Receptors, Drug; D012486:Salmonella typhimurium / Q000378:metabolism*; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D005971:Glutamates; D011422:Propionates; D011955:Receptors, Drug; D001224:Aspartic Acid; D004492:Edetic Acid; D003544:Cysteic Acid; D004229:Dithiothreitol