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Different binding sites for entry and exit of amino acids in whole cells of Mycobacterium phlei


, : Different binding sites for entry and exit of amino acids in whole cells of Mycobacterium phlei. Journal of Bacteriology 130(2): 729-735

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.


Accession: 005151934

PMID: 263821

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Related references

Deves R.; Brodie A.F., 1980: The entry process as the target for energy input in active transport of amino acids in mycobacterium phlei. Federation Proceedings 39(6): ABSTRACT 2908

Prasad, R.; Kalra, V.K.; Brodie, A.F., 1976: Different mechanisms of energy coupling for transport of various amino acids in cells of Mycobacterium phlei. Whole cells of Mycobacterium phlei were shown to actively accumulate proline, leucine, lysine, tryptophan, histidine, glutamine, and glutamic acid to different steady state levels. The transport of proline, in contrast to that of other amino acids...

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