Multiple Oxidative Routes towards the Maturation of Nosiheptide

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. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.