• Title/Summary/Keyword: Structures of biotransformed xanthostatin

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N-Acetylglycine Side Chain is Critical for the Antimicrobial Activity of Xanthostatin

  • Kim, Si-Kwan;Ubukata, Makoto;Isono, Kiyoshi
    • Journal of Microbiology and Biotechnology
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    • v.13 no.6
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    • pp.998-1000
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    • 2003
  • This study was carried out to elucidate the mode of bacteriostatic property of xanthostatin (XS), a novel depsipeptide antibiotic with an N-acetylglycine side chain and selective antimicrobial activity against Xanthomonas spp. Two biotransformed XSs were isolated by the treatment of XS with the cell lysate of Xanthomonas campestris pv. citri, a solvent partition, preparative TLC, and HPLC. Structure determination of those two biotransformed XSs demonstrated deletion of the N-acetylglycine side chain. Noteworthily, they showed no antimicrobial activity against Xanthomonas spp. This result suggests that the N-acetylglycine side chain plays a critical role in the antimicrobial activity of XS, and that the bacteriostatic property of XS is due to susceptibility of the ester bond between the hexadepsipeptide nucleus and the N-acetylglycine side chain to hydrolytic enzyme(s) produced by Xanthomonas spp.