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expansion of the substrate specificity and enhancment of biosynthesis of polyhydroxyalkanoate by site-specific mutagenesis. Mutated PhaC1s are coexpressed with beta-ketothiolase and acetoacetyl-CoA reductase to supply sufficient short-chain length (R)-3-hydroxyacyl-CoA as a substrate. Mutation L484V remarkably enhances the monomer ratio of (R)-3-hydroxybutyrate in a polyhydroxyalkanoate accumulation experiment. Val is the most favorable amino acid for incorporating (R)-3-hydroxybutyrate unit synthesis. A single mutation at Q481M, S482G and A547V obviously increases polyhydroxyalkanoate yields. Q481M and S482G enhance the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
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