Mutations to the active site of 3-ketoacyl-ACP synthase III (FabH) increase polyhydroxyalkanoate biosynthesis in transgenic Escherichia coli

Abstract

Polyhydroxyalkanoate (PHA) production has been enhanced with engineered 3-ketoacyl-ACP synthase III (FabH) enzymes that accept diverse fatty acyl-ACP substrates and convert them to fatty acyl-CoA substrates for polymerization by PHA synthase enzymes resulting in the production of diverse polymers. Two mutations in the monomer supplying enzyme FabH, His244Ala and the Asn274Ala, were investigated to assess the impact of these mutations on PHA monomer production. PHA production increased more than six-fold with the mutation His244Ala in the FabH enzyme. Engineering of the FabH enzyme for improved PHA monomer supply led to a more productive system for PHA copolymer production.