Identification of Novel Irreversible Inhibitors of UDP-N-Acetylglucosamine Enolpyruvyl Transferase (MurA) from Haemophilus influenzae

분야
자연과학 > 생물
저자
( Seong Gu Han ) , ( Won Kyu Lee ) , ( Bong Suk Jin ) , ( Ki In Lee ) , ( Hyeong Ho Lee ) , ( Yeon Gyu Yu )
발행기관
한국미생물생명공학회(구 한국산업미생물학회)
간행물정보
Journal of Microbiology and Biotechnology 2013년, 제23권 제3호, 329~334페이지(총6페이지)
파일형식
05212225.pdf [무료 PDF 뷰어 다운로드]
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    영문초록
    Uridinediphospho-N-acetylglucosamine enolpyruvyl transferase (MurA, E.C. 2.5.1.7) is an essential bacterial enzyme that catalyzes the first step of the cell wall biosynthetic pathway, which involves the transfer of an enolpyruvyl group from phosphoenolpyruvate to uridinediphospho-Nacetylglucosamine. In this study, novel inhibitors of Haemophilus influenzae MurA (Hi MurA) were identified using high-throughput screening of a chemical library from the Korea Chemical Bank. The identified compounds contain a quinoline moiety and have much lower effective inhibitory concentrations (IC50) than fosfomycin, a wellknown inhibitor of MurA. These inhibitors appear to covalently modify the sulfhydryl group of the active site cysteine (C117), since the C117D mutant Hi MurA was not inhibited by these compounds and excess dithiothreitol abolished their inhibitory activities. The increased mass value of Hi MurA after treatment with the identified inhibitor further confirmed that the active-site cysteine residue of Hi MurA is covalently modified by the inhibitor.
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