Opposed effects of enzymatic gliotoxin N- and S-methylations.

@article{Scharf2014OpposedEO,
  title={Opposed effects of enzymatic gliotoxin N- and S-methylations.},
  author={Daniel H Scharf and Andreas Habel and Thorsten Heinekamp and Axel A. Brakhage and Christian Hertweck},
  journal={Journal of the American Chemical Society},
  year={2014},
  volume={136 33},
  pages={11674-9}
}
Gliotoxin (1), a virulence factor of the human pathogenic fungus Aspergillus fumigatus, is the prototype of epipoly(thiodioxopiperazine) (ETP) toxins. Here we report the discovery and functional analysis of two methyl transferases (MTs) that play crucial roles for ETP toxicity. Genome comparisons, knockouts, and in vitro enzyme studies identified a new S-adenosyl-l-methionine-dependent S-MT (TmtA) that is, surprisingly, encoded outside the gli gene cluster. We found that TmtA irreversibly… CONTINUE READING
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