Mutations to the active site of 3-ketoacyl-ACP synthase III (FabH) increase polyhydroxyalkanoate biosynthesis in transgenic Escherichia coil(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
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概要
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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.
著者
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Mueller Alexander
State University Of New York College Of Environmental Science And Forestry Department Of Chemistry
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Nomura Christopher
State University Of New York College Of Environmental Science And Forestry Department Of Chemistry
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Nomura Christopher
State University Of New York College Of Environmental Science And Forestry
関連論文
- Mutations to the active site of 3-ketoacyl-ACP synthase III (FabH) increase polyhydroxyalkanoate biosynthesis in transgenic Escherichia coil(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Precise control of repeating unit composition in biodegradable poly(3-hydroxyalkanoate) polymers synthesized by Escherichia coli(MICROBIAL PHYSIOLOGY AND BIOTECHNOLOGY)