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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.
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