Abstract
The functional diversity and catalytic potential of type III polyketide synthases are remarkable. The enzymes catalyze iterative decarboxylative condensations of malonyl unit (Claisen-type C-C bond formation) with a CoA-linked starter molecule to produce structurally diverse, pharmaceutically important secondary metabolites. Recent studies have revealed intimate structural details of the enzyme reactions, which enabled the precursor-directed and structure-based engineered biosynthesis of unnatural polyketides.
Keywords: Type III polyketide synthase, enzymatic synthesis, precursor-directed biosynthesis, structure-based engineered biosynthesis, combinatorial biosynthesis
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