MmfL catalyses formation of a phosphorylated butenolide intermediate in methylenomycin furan biosynthesis.
MmfL catalyses formation of a phosphorylated butenolide intermediate in methylenomycin furan biosynthesis.
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DOI:
10.1039/d0cc05658h
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发表时间:
2020-11
影响因子:
4.9
通讯作者:
Shanshan Zhou;Nicolas Malet;Lijiang Song;C. Corre;G. Challis
中科院分区:
文献类型:
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作者:
Shanshan Zhou;Nicolas Malet;Lijiang Song;C. Corre;G. Challis
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.