In a cell-free system from Bacillus subtilis B3, ATP–Pi 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.
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Research Article| June 01 1972
Peptides from a mycobacillin-synthesizing cell-free system
S. Sengupta ;
Biochem J (1972) 128 (1): 47–52.
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S. Sengupta, S. K. Bose; Peptides from a mycobacillin-synthesizing cell-free system. Biochem J 1 June 1972; 128 (1): 47–52. doi: https://doi.org/10.1042/bj1280047
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