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Peptides from a mycobacillin-synthesizing cell-free system.

ABSTRACT: 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.

SUBMITTER: Sengupta S

PROVIDER: S-EPMC1173568 | biostudies-other | 1972 Jun

REPOSITORIES: biostudies-other

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Stereoconfiguration of amino acids in peptides from a mycobacillin-synthesizing cell-free system.

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