1887

Abstract

Thirteen mycobacillin-negative (My) mutants of B were isolated from an auxotrophically tagged mycobacillin producer organism. The wild-type producer, three feeble producers and three strictly My mutants did not accumulate any ninhydrin-positive peptide in the culture medium while the remaining seven My mutants did accumulate ten such peptides whose amino acid composition indicated that there might be only three different peptides. The -terminal and C-terminal amino acid residues implicated one of these peptides as a pentapeptide intermediate in mycobacillin synthesis; this was further confirmed by its molecular weight and sequence. Studies on cell-free synthesis showed that only the enzyme system from the wild-type strain synthesized mycobacillin while the defective ones from all the My mutants synthesized one and the same pentapeptide as found in the culture broth of some of the mutants. Further studies in which the enzymes responsible for mycobacillin synthesis by cell-free extracts were separated into three fractions, A, B and C, showed that seven of the mutants were defective in fraction B whereas the three other mutants had defects in both fractions B and C. Thus the pentapeptide Pro→Asp→Glu→Tyr→Asp appears to be implicated in mycobacillin biosynthesis.

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1985-01-01
2021-10-20
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