Báo cáo khoa học: Role of K22 and R120 in the covalent binding of the antibiotic fosfomycin and the substrate-induced conformational change in UDP-N-acetylglucosamine enol pyruvyl transferase
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UDP-N-acetylglucosamineenolpyruvyl transferase (MurA),catalyzes the first step in the biosynthesis of peptidoglycan,involving the transfer of the intactenolpyruvyl moiety fromphosphoenolpyruvate to the 3¢-hydroxyl group of UDP-N-acetylglucosamine (UDPNAG). The enzyme is irreversiblyinhibited by the antibiotic fosfomycin. The inactivation iscaused by alkylation of a highly conserved cysteine residue(C115) that participates in the binding of phos-phoenolpyruvate.
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Báo cáo khoa học: Role of K22 and R120 in the covalent binding of the antibiotic fosfomycin and the substrate-induced conformational change in UDP-N-acetylglucosamine enol pyruvyl transferase
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: Role of K22 and R120 in the covalent binding of the antibiotic fosfomycin and the substrate-induced conformational change in UDP-N-acetylglucosamine enol pyruvyl transferase
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