Improved production of L-lysine by over-expression of Meso-diaminopimelate decarboxylase enzyme of Corynebacterium glutamicum in Escherichia coli

Pak J Biol Sci. 2010 May 15;13(10):504-8. doi: 10.3923/pjbs.2010.504.508.


The aim of this study is over-expression of Meso-diaminopimelate decarboxylase enzyme (EC and enhancement of L-lysine production rate. The C. glutamicum LysA gene which encodes a Meso-diaminopimelate decarboxylase was cloned in E. coli. The cloned gene was sequenced; it encodes a 445 amino acids protein with molecular weight of 47 kD. Expression of the LysA gene in E. coli resulted in an increase in Meso-diaminopimelate decarboxylase activity, correlated with the presence in sodium dodecyl sulfate-polyacrylamid gels of a clear protein band that corresponds to this enzyme. The induction of cloned gene by IPTG has been shown to have an inhibitory effect on cell growth due to over-expression of the cloned gene. A two fold increase in lysine production rate was observed after introduction of the cloned gene into E. coli.

MeSH terms

  • Amino Acids / chemistry
  • Bacterial Proteins / genetics
  • Biotechnology / methods*
  • Carboxy-Lyases / biosynthesis*
  • Carboxy-Lyases / genetics
  • Carboxy-Lyases / metabolism
  • Cloning, Molecular
  • Corynebacterium glutamicum / enzymology*
  • Corynebacterium glutamicum / genetics
  • DNA / chemistry
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Gene Expression Regulation, Bacterial
  • Lysine / metabolism*
  • Molecular Weight
  • Plasmids / metabolism
  • Polymerase Chain Reaction / methods
  • Time Factors


  • Amino Acids
  • Bacterial Proteins
  • DNA
  • Carboxy-Lyases
  • LysA protein, Bacteria
  • diaminopimelic acid decarboxylase
  • Lysine