Biosynthesis of depsipeptide mycotoxins in Fusarium

  • Till Hornbogen
  • Mirko Glinski
  • Rainer Zocher

Abstract

The cyclic hexadepsipeptide enniatin is known as a phytopathogenic compound from Fusaria causing necrosis and wilt. The molecule consists of three alternating residues each of a branched chain amino acid and D-hydroxyisovaleric acid (D-Hiv). Enniatins are synthesized by a 347 kDa multienzyme (enniatin synthetase) via a thiol template mechanism. The corresponding gene esynl has an open reading frame of 9393 nucleotides and harbours two modules, one responsible for D-hydroxy acid activation and one for L-amino acid activation with an integrated N-methyltransferase domain. Such methyltransferases build an homologous group among N-methyl peptide synthetases. Enniatins are synthesized by step-wise condensation of dipeptidol building blocks in an iterative manner resembling fatty acid synthesis. A key enzyme in enniatin biosynthesis is the NADPH-dependent D-2-hydroxyisovalerate dehydrogenase, that supplies enniatin synthetase with D-Hiv. Enniatins contribute to the wilt toxic character of Fusaria. Virulence was significantly reduced in F. avenaceum after disruption of the esynl gene.

Key words:

enniatin synthetase Fusarium N-methylated cyclodepsipeptides nonribosomal peptide synthesis phytopathogenic 

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Copyright information

© Springer Science+Business Media Dordrecht 2002

Authors and Affiliations

  • Till Hornbogen
    • 1
  • Mirko Glinski
    • 1
  • Rainer Zocher
    • 1
  1. 1.Fakultät II, Institut für Chemie, Arbeitsgruppe Biochemie und Molekulare BiologieTechnische Universtät BerlinBerlinGermany

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