Structural insights of the MenD from Escherichia coli reveal ThDP affinity

Amit Priyadarshi, Yasar Saleem, Ki Hyun Nam, Key Sun Kim, Sam Yong Park, Eunice Eun Kyeong Kim, Kwang Yeon Hwang

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


MenD (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate) synthase belongs to the superfamily of thiamin diphosphate-dependent decarboxylases, which converts isochorismate and 2-oxoglutarate to SHCHC, pyruvate, and carbon dioxide. Here, we report the first crystal structure of apo-MenD from Escherichia coli determined in tetragonal crystal form. The subunit displays the typical three-domain structure observed for ThDP-dependent enzymes. Analytical gel filtration shows that EcMenD behaves as a dimer as well as a tetramer. Circular dichroism and isothermal calorimetry results confirm EcMenD dependency on ThDP, which concomitantly helps to stabilize with better configuration.

Original languageEnglish
Pages (from-to)797-801
Number of pages5
JournalBiochemical and biophysical research communications
Issue number4
Publication statusPublished - 2009 Mar 20


  • Decarboxylase
  • MenD
  • Menaquinone
  • Oxoglutarate
  • ThDP
  • Transferase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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