Engineering Escherichia coli for efficient production of 5-aminolevulinic acid from glucose

Metab Eng. 2011 Sep;13(5):492-8. doi: 10.1016/j.ymben.2011.05.003. Epub 2011 May 23.

Abstract

5-Aminolevulinic acid (ALA) recently received much attention due to its potential applications in many fields. In this study, we developed a metabolic strategy to produce ALA directly from glucose in recombinant Escherichia coli via the C5 pathway. The expression of a mutated hemA gene, encoding a glutamyl-tRNA reductase from Salmonella arizona, significantly improved ALA production from 31.1 to 176mg/L. Glutamate-1-semialdehyde aminotransferase from E. coli was found to have a synergistic effect with HemA(M) from S. arizona on ALA production (2052mg/L). In addition, we identified a threonine/homoserine exporter in E. coli, encoded by rhtA gene, which exported ALA due to its broad substrate specificity. The constructed E. coli DALA produced 4.13g/L ALA in modified minimal medium from glucose without adding any other co-substrate or inhibitor. This strategy offered an attractive potential to metabolic production of ALA in E. coli.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aldehyde Oxidoreductases* / biosynthesis
  • Aldehyde Oxidoreductases* / genetics
  • Aminolevulinic Acid / metabolism*
  • Bacterial Proteins* / biosynthesis
  • Bacterial Proteins* / genetics
  • Escherichia coli* / genetics
  • Escherichia coli* / growth & development
  • Escherichia coli* / metabolism
  • Glucose / genetics
  • Glucose / metabolism*
  • Mutation
  • Organisms, Genetically Modified* / genetics
  • Organisms, Genetically Modified* / growth & development
  • Organisms, Genetically Modified* / metabolism
  • Salmonella arizonae* / enzymology
  • Salmonella arizonae* / genetics

Substances

  • Bacterial Proteins
  • Aminolevulinic Acid
  • Aldehyde Oxidoreductases
  • glutamyl tRNA reductase
  • Glucose