Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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5-Aminolevulinic Acid Biosynthesis in Escherichia coli Coexpressing NADP-dependent Malic Enzyme and 5-Aminolevulinate Synthase

  • Shin, Jeong-Ah (Department of Biotechnology, The Catholic University of Korea) ;
  • Kwon, Yeong-Deok (Department of Biotechnology, The Catholic University of Korea) ;
  • Kwon, Oh-Hee (Department of Biotechnology, The Catholic University of Korea) ;
  • Lee, Heung-Shick (Department of Biotechnology and Bioinformatics, Korea University) ;
  • Kim, Pil (Department of Biotechnology, The Catholic University of Korea)
  • Published : 2007.09.30
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Abstract

5-Aminolevulinate (ALA) synthase (E.C. 2.3.1.37), which mediates the pyridoxal phosphate-dependent condensation of glycine and succinyl-CoA, encoded by the Rhodobacter sphaeroides hemA gene, enables Escherichia coli strains to produce ALA at a low level. To study the effect of the enhanced C4 metabolism of E. coli on ALA biosynthesis, NADP-dependent malic enzyme (maeB, E.C. 1.1.1.40) was coexpressed with ALA synthase in E. coli. The concentration of ALA was two times greater in cells coexpressing maeB and hemA than in cells expressing hemA alone under anaerobic conditions with medium containing glucose and glycine. Enhanced ALA synthase activity via coupled expression of hemA and maeB may lead to metabolic engineering of E. coli capable of large-scale ALA production.

Keywords

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