MmfL catalyses formation of a phosphorylated butenolide intermediate in methylenomycin furan biosynthesis
| Autor: | Christophe Corre, Lijiang Song, Gregory L. Challis, Shanshan Zhou, Nicolas Malet |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Stereochemistry
010402 general chemistry Thioester 01 natural sciences Catalysis Structure-Activity Relationship chemistry.chemical_compound 4-Butyrolactone Bacterial Proteins Biosynthesis Furan Escherichia coli Materials Chemistry QD Phosphorylation Furans Dihydroxyacetone phosphate Butenolide chemistry.chemical_classification biology 010405 organic chemistry Streptomyces coelicolor Metals and Alloys Substrate (chemistry) Gene Expression Regulation Bacterial General Chemistry biology.organism_classification Streptomyces Methylenomycin Anti-Bacterial Agents Biosynthetic Pathways 0104 chemical sciences Surfaces Coatings and Films Electronic Optical and Magnetic Materials chemistry Ceramics and Composites Peptides |
| ISSN: | 1364-548X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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