Acyl carrier protein: structure–function relationships in a conserved multifunctional protein family

摘要: Acyl carrier protein (ACP) is a universal and highly conserved of acyl intermediates during fatty acid synthesis. In yeast mammals, ACP exists as separate domain within large multifunctional synthase polyprotein (type I FAS), whereas it small monomeric in bacteria plastids II FAS). Bacterial ACPs are also donors for synthesis variety products, including endotoxin acylated homoserine lactones involved quorum sensing; the distinct essential nature these processes growth pathogenesis make ACP-dependent enzymes attractive antimicrobial drug targets. Additionally, homologues key components production secondary metabolites such polyketides nonribosomal peptides. Many exhibit characteristic structural features natively unfolded proteins vitro, with dynamic flexible conformation dominated by 3 parallel alpha helices that enclose thioester-linked group attached to phosphopantetheine prosthetic group. may be influenced divalent cations interaction partner through its "recognition" helix II, properties ability alternately sequester groups deliver them active sites enzymes. This review highlights recent progress defining how related multiple roles metabolism.