Shepo Shi, Hiroyuki Morita, Kiyofumi Wanibuchi, Yuusuke Mizuuchi, Hiroshi Noguchi and Ikuro Abe Pages 250 - 266 ( 17 )
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.
Type III polyketide synthase, enzymatic synthesis, precursor-directed biosynthesis, structure-based engineered biosynthesis, combinatorial biosynthesis
University of Shizuoka, School of Pharmaceutical Sciences, 52-1 Yada, Shizuoka 422-8526, Japan.