Abstract
A soluble enzyme complex participates in the biosynthesis of bacitracin which is an antibiotic dodecapeptide produced by a strain of Bacillus licheniformis and the peptide is synthesized from amino acids bdund to enzyme protein through thioester linkages [ 1,2] . These features of bacitracin synthetase resemble those in the biosynthesis of gramicidin S and tyrocidine [3]. Recently, it was reported that gramicidin S and tyrocidine synthetases contained one and two moles of 4’-phosphopantetheine pr mole of synthetase, respectively [4,5], and that phosphopantetheine arm participated in peptide chain elongation [6]. Bacitracin synthetase has beeri separated into two complementary fractions (Peaks I and II) by column chromatography on hydroxyapatite [2]. The present work demonstrates that Peak II fraction was further separated into two components and that each of the three components responsible for bacitracin biosynthesis contains approximately one equivalent of 4’-phosphopantetheine.
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