Korean Journal of Crystallography (한국결정학회지)

Korean Crystallographic Association (한국결정학회)
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A Docking Study of UDP-N-Acetylglucosamine Enolpyruvyl Transferase from Haemophilus influenzae in Complex with Inhibitors

  • Yoon, Hye-Jin (Department of Chemistry, College of Natural Sciences, Seoul National University) ;
  • Mikami, Bunzo (Laboratory of Quality Design and Exploitation, Division of Agronomy and Horticultural Science, Graduate School of Agriculture, Kyoto University) ;
  • Park, Hyun-Ju (College of Pharmacy, Sungkyunkwan University) ;
  • Yoo, Ja-Kyung (College of Pharmacy, Sungkyunkwan University) ;
  • Suh, Se-Won (Department of Chemistry, College of Natural Sciences, Seoul National University)
  • Published : 2007.12.31
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Abstract

UDP-N-acetylglucosamine enolpyruvyl transferase (MurA; EC 2.5.1.7) catalyzes the first committed step of peptidoglycan biosynthesis in bacteria, i.e., transfer of enolpyruvate from phosphoenolpyruvate to UDP-N-acetyl-glucosamine. Because the crystallization condition contained a high concentration of ammonium sulfate, our inhibitor binding studies were not successful. Therefore, we employed a docking approach to investigate the inhibitor binding. Our results will be useful in structure-based design of specific inhibitors of MurA for antibacterial discovery.

Keywords

References

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