1-5-dihydro-fad and indirubin

Terpenoid natural products comprise a wide range of molecular architectures that typically result from C-C bond formations catalysed by classical type I/II terpene cyclases. However, the molecular diversity of biologically active terpenoids is substantially increased by fully unrelated, non-canonical terpenoid cyclases. Their evolutionary origin has remained enigmatic. Here we report the in vitro reconstitution of an unusual flavin-dependent bacterial indoloterpenoid cyclase, XiaF, together with a designated flavoenzyme-reductase (XiaP) that mediates a key step in xiamycin biosynthesis. The crystal structure of XiaF with bound FADH

Topics: Bacteria; Bacterial Proteins; Cyclization; Flavin-Adenine Dinucleotide; Hydroxylation; Inactivation, Metabolic; Indigo Carmine; Indoles; Lyases; Molecular Structure; Phylogeny; Terpenes; Xenobiotics