Chanoclavine synthase operates by an NADPH-independent superoxide mechanism.

ABSTRACT: More than ten ergot alkaloids comprising both natural and semi-synthetic products are used to treat various diseases^1,2. The central C ring forms the core pharmacophore for ergot alkaloids, giving them structural similarity to neurotransmitters, thus enabling their modulation of neurotransmitter receptors³. The haem catalase chanoclavine synthase (EasC) catalyses the construction of this ring through complex radical oxidative cyclization⁴. Unlike canonical catalases, which catalyse H₂O₂ disproportionation^5,6, EasC and its homologues represent a broader class of catalases that catalyse O₂-dependent radical reactions^4,7. We have elucidated the structure of EasC by cryo-electron microscopy, revealing a nic

SUBMITTER: Chen CC 

PROVIDER: S-EPMC12003167 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature