[Transport of phenylalanine and tyrosine in Brevibacterium linens: specificity and incorporation into proteins].
The specificity of phenylalanine and tyrosine carriers was investigated using actively metabolizing cells of Brevibacterium linens. The cellular protein synthesis of resting cells was very weakly inhibited, even with high concentrations of chloramphenicol or tetracycline. The nonaromatic amino acids were weak inhibitors for these carriers, while fluorinate analogues of phenylalanine and tyrosine were very potent competitive inhibitors. In practice these analogues cannot be used to replace amino acids to evaluate transport without incorporation because they are incorporated in cellular proteins.
D000596:Amino Acids / Q000494:pharmacology; D001426:Bacterial Proteins / Q000096:biosynthesis*; D001692:Biological Transport / Q000187:drug effects; D001951:Brevibacterium / Q000187:drug effects / Q000378:metabolism*; D002701:Chloramphenicol / Q000633:toxicity; D007700:Kinetics; D010649:Phenylalanine / Q000378:metabolism*; D014176:Protein Biosynthesis / Q000187:drug effects; D013752:Tetracycline / Q000633:toxicity; D014443:Tyrosine / Q000378:metabolism*
D000596:Amino Acids; D001426:Bacterial Proteins; D014443:Tyrosine; D010649:Phenylalanine; D002701:Chloramphenicol; D013752:Tetracycline
Le transport de la phénylalanine et de la tyrosine chez Brevibacterium linens: spécificité et incorporation dans les protéines.