Organic & Biomolecular Chemistry · 2013 · 50 citations · 56 references
PharmacyBiotechnologyMolecular BiologyEnzymologyMetabolic EngineeringSynthetic BiologyCatalytic MechanismsCombinatorial BiosynthesisEnzyme DesignEnzyme-substrate RecognitionMetabolic Pathway EngineeringPolyketide BiosynthesisExtender Unit IncorporationIn Vivo DiversificationModular Polyketide BiosynthesisPolyketide Synthase EngineeringPolyketide Synthase PathwaysSubstrate Binding SpecificityTailoring Enzyme EngineeringType I Polyketide Synthases
Combinatorial biosynthesis approaches that involve modular type I polyketide synthases (PKSs) are proven strategies for the synthesis of polyketides. In general however, such strategies are usually limited in scope and utility due to the restricted substrate specificity of polyketide biosynthetic machinery. Herein, a panel of chemo-enzymatically synthesized acyl-CoA's was used to probe the promiscuity of a polyketide synthase. Promiscuity determinants were dissected, revealing that the KS is remarkably tolerant to a diverse array of extender units, while the AT likely discriminates between extender units that are native to the producing organism. Our data provides a clear blueprint for future enzyme engineering efforts, and sets the stage for harnessing extender unit promiscuity by employing various in vivo polyketide diversification strategies.
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Robert McDaniel, Arinthip Thamchaipenet, Claes Gustafsson et al. · Proceedings of the National Academy of Sciences · 1999 · 461 citations
Site-specific protein labeling by Sfp phosphopantetheinyl transferase
Jun Yin, Alison J. Lin, David E. Golan et al. · Nature Protocols · 2006 · 341 citations