Different binding sites for entry and exit of amino acids in whole cells of Mycobacterium phlei.
On the basis of mutual inhibition of uptake with different amino acids in whole cells of Mycobacterium phlei, it was demonstrated that the binding site of proline was different from those of all other amino acids studied. Other groups of amino acids share a common binding site: lysine, histidine, and arginine; valine, leucine, and isoleucine; tryptophan, tyrosine, and phenylalanine; glutamic acid and aspartic acid. The exit and entry processes were studied for proline, glutamine, and glutamic acid. It was observed that in each case the entry and exit processes were mediated by different membrane sites.
D000596:Amino Acids / Q000378:metabolism*; D001665:Binding Sites; D001692:Biological Transport; D005971:Glutamates / Q000378:metabolism; D018698:Glutamic Acid; D005973:Glutamine / Q000378:metabolism; D007700:Kinetics; D009161:Mycobacterium / Q000378:metabolism*; D009168:Mycobacterium phlei / Q000378:metabolism*; D011392:Proline / Q000378:metabolism; D013329:Structure-Activity Relationship
D000596:Amino Acids; D005971:Glutamates; D005973:Glutamine; D018698:Glutamic Acid; D011392:Proline
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