Analysis of in vivo substrate specificity of the PHA synthase from Ralstonia eutropha: formation of novel copolyesters in recombinant Escherichia coli.

@article{Antnio2000AnalysisOI,
  title={Analysis of in vivo substrate specificity of the PHA synthase from Ralstonia eutropha: formation of novel copolyesters in recombinant Escherichia coli.},
  author={Regina Vasconcellos Ant{\^o}nio and Alexander Steinb{\"u}chel and Bernd H A Rehm},
  journal={FEMS microbiology letters},
  year={2000},
  volume={182 1},
  pages={
          111-7
        }
}
In order to investigate the in vivo substrate specificity of the type I polyhydroxyalkanoate (PHA) synthase from Ralstonia eutropha, we functionally expressed the PHA synthase gene in various Escherichia coli mutants affected in fatty acid beta-oxidation and the wild-type. The PHA synthase gene was expressed either solely (pBHR70) or in addition to the R. eutropha genes encoding beta-ketothiolase and acetoacetyl-coenzyme A (CoA) reductase comprising the entire PHB operon (pBHR68) as well as in… CONTINUE READING

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