Aldolase; part of the gene cluster that mediates the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid with a unique, fused spirobicyclic ring system .
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Aldolase; part of the gene cluster that mediates the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid with a unique, fused spirobicyclic ring system (PubMed:20534346). The first step of the pathway is the production of the malonamoyl-CoA starter unit for the polyketide synthase vrtA (PubMed:20534346). The aldolase vrtJ may be involved in the synthesis of the malonamate substrate for malonamoyl-CoA synthetase vrtB (PubMed:20534346). The polyketide synthase vrtA then may utilize the malonamoyl-CoA starter unit, followed by sequential condensation of eight malonyl-CoA units to form the polyketide backbone (PubMed:20534346). The cyclization of the last ring could be mediated by the lactamase-like protein vrtG (PubMed:20534346). The proposed post-PKS tailoring steps are an hydroxylation at C5 catalyzed the cytochrome P450 monooxygenase vrtE, an hydroxylation at C12a catalyzed by VrtH and/or VrtI, and an O-methylation by the O-methyltransferase vrtF (PubMed:20534346, PubMed:24161266). VrtC is then proposed to catalyze the transfer of a geranyl group synthesized by vrtD to the aromatic C ring of the tetracyclic polyketide intermediate of viridicatumtoxin to yield previridicatumtoxin (PubMed:20534346). Finally, the cytochrome P450 monooxygenase vrtK catalyzes the spirocyclization of the geranyl moeity of previridicatumtoxin to afford viridicatumtoxin (PubMed:24161266).