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Keywords:

  • biosynthesis;
  • enamine dealkylation;
  • hydroxylation;
  • nosiheptide;
  • p450 mono-oxygenases
Thumbnail image of graphical abstract

Three oxidative routes: Two cytochrome P450-like mono-oxygenases cooperate in the biosynthesis of nosiheptide (Nos): NosB catalyzes hydroxylation of the Glu6 γ-position, whereas NosC hydroxylates the Pyr3 position, thus enabling cleavage of the bis-Dha tail by NosA. Combining the polysubstrate specificity of NosB and NosC and the function of NosA generates three oxidative routes in nosiheptide maturation.