Heterologous expression of the acyl–acyl carrier protein thioesterase gene from the plant Umbellularia californica mediates polyhydroxyalkanoate biosynthesis in recombinant Escherichia ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2001-03

AUTHORS

Bernd H. Rehm, Alexander Steinbüchel

ABSTRACT

The acyl-acyl carrier protein (ACP) thioesterase cDNA from the plant Umbellularia californica was functionally expressed in various recombinant Escherichia coli strains in order to establish a new metabolic route toward medium-chain-length polyhydroxyalkanoate (PHA(MCL)) biosynthesis from non-related carbon sources. Coexpression of the PHA synthase genes from Ralstonia eutropha and Pseudomonas aeruginosa, or only the PHA synthase gene from P. aeruginosa, respectively, showed PHA(MCL) accumulation when the type II PHA synthase from P. aeruginosa was produced. Both wild-type E. coli and various fad mutants were investigated; and only when the beta-oxidation pathway was impaired PHA(MCL) accumulation from gluconate was observed, contributing to about 6% of cellular dry weight. Thus coexpression of type II PHA synthase gene with cDNA encoding the medium-chain acyl-ACP thioesterase from U. californica established a new PHA(MCL) biosynthesis pathway, connecting fatty acid de novo biosynthesis with fatty acid beta-oxidation, using a non-related carbon source. More... »

PAGES

205-209

Journal

TITLE

Applied Microbiology and Biotechnology

ISSUE

2

VOLUME

55

Author Affiliations

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s002530000541

    DOI

    http://dx.doi.org/10.1007/s002530000541

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1019517897

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/11330715


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