Peptides from a mycobacillin-synthesizing cell-free system.
In a cell-free system from Bacillus subtilis B(3), ATP-P(i) exchange was catalysed by l-proline at a pH optimum of 7.2. Further stimulation by component amino acids of mycobacillin was inhibited by deprivation from the synthesizing system of even a single amino acid occurring at any point of the cyclic peptide. This inhibition, however, decreased with the distance in the molecule of the given amino acid from l-proline. Peptides containing respectively two, three, four, five and six amino acids were isolated from the mycobacillin-synthesizing system by an amino acid-deprivation technique. The amino acid composition of these peptides and also their N- and C-terminal amino acid residues were the same as those of peptides that would be obtained if mycobacillin synthesis occurred starting from l-proline and was interrupted at various points along the polypeptide chain.
D000255:Adenosine Triphosphate; D000596:Amino Acids / Q000032:analysis; D000935:Antifungal Agents / Q000096:biosynthesis*; D001412:Bacillus subtilis; D002247:Carbon Isotopes; D002474:Cell-Free System; D011756:Diphosphates; D006863:Hydrogen-Ion Concentration; D010456:Peptides, Cyclic / Q000096:biosynthesis*; D011392:Proline
D000596:Amino Acids; D000935:Antifungal Agents; D002247:Carbon Isotopes; D011756:Diphosphates; D010456:Peptides, Cyclic; D000255:Adenosine Triphosphate; D011392:Proline