Identification of a novel sesquiterpene biosynthetic machinery involved in astellolide biosynthesis

Farnesyl pyrophosphate
DOI: 10.1038/srep32865 Publication Date: 2016-09-15T09:12:08Z
ABSTRACT
Abstract Esterified drimane-type sesquiterpene lactones such as astellolides display various biological activities and are widely produced by plants fungi. Given their low homology to known cyclases, the genes responsible for biosynthesis have not been uncovered yet. Here, we identified astellolide gene cluster from Aspergillus oryzae discovered a novel biosynthetic machinery consisting of AstC, AstI, AstK. All these enzymes annotated haloacid dehalogenase-like hydrolases, whereas AstC also contains DxDTT motif conserved in class II diterpene cyclases. Based on enzyme reaction analyses, found that catalysed protonation-initiated cyclisation farnesyl pyrophosphate into drimanyl pyrophosphate. This was successively dephosphorylated AstI AstK produce drim-8-ene-11-ol. Moreover, characterised unique non-ribosomal peptide synthetase, AstA, esterifying aryl acids lactones. In this study, highlight new route producing its esterified derivative. Our findings shed light identification sesquiterpenes via genome mining.
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