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Oligopeptide transport in proline peptidase mutants of Salmonella typhimurium
Journal of Biological Chemistry
Investigations of peptide transport in Salmonella typhimurium are presented. A strain designated proB25, a proline auxotroph, grew on a variety of di, tri-, and tetrapeptides containing proline. In contrast (Pro)6, peptides acylated on the NH2 terminus and Ala-Pro-D-Ala did not satisfy the nutritional requirement of proB25 for proline because they were not transported. A derivative of proB25, strain TN87, deficient in a proline aminopeptidase and an X-Pro dipeptidase, was able to utilize onlypmid:783159 fatcat:xrnnxem5bjegxjmqduvjrzgi2e