MmfL catalyses formation of a phosphorylated butenolide intermediate in methylenomycin furan biosynthesis. Issue 92 (4th November 2020)

• Record Type: Journal Article
• Authors: Zhou, Shanshan; Malet, Nicolas R.; Song, Lijiang; Corre, Christophe; Challis, Gregory L.
• Is Part Of: Chemical communications. Volume 56:Issue 92(2020)
• Page Start: 14443
• Page End: 14446
• Publication Date: 2020-11-04
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/d0cc05658h
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : MmfL forms phosphorylated butenolides that undergo dephosphorylation and rearrangement to yield methylenomycin furan (MMF) signalling molecules that induce antibiotic production in Streptomyces coelicolor . Abstract : Using a combination of a synthetic substrate analogue and product standard, MmfL, a homologue of the γ-butyrolactone biosynthetic enzyme AfsA, was shown to catalyse the condensation of dihydroxyacetone phosphate with a β-ketoacyl thioester to form a phosphorylated butenolide intermediate in the biosynthesis of the methylenomycin furans, which induce methlenomycin antibiotic production in Streptomyces coelicolor A3(2). AfsA homologues are also involved in the biosynthesis of 2-akyl-4-hydroxy-3-methyl butenolide inducers of antibiotic production in other Streptomyces species, indicating that diverse signalling molecules are assembled from analogous phosphorylated butenolide intermediates.