Centre for Computational Chemistry, School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK.
School of Cellular and Molecular Medicine, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
Chem Commun (Camb). 2020 Jun 23;56(50):6874-6877. doi: 10.1039/d0cc02520h.
MCR (mobile colistin resistance) enzymes catalyse phosphoethanolamine (PEA) addition to bacterial lipid A, threatening the "last-resort" antibiotic colistin. Molecular dynamics and density functional theory simulations indicate that monozinc MCR supports PEA transfer to the Thr285 acceptor, positioning MCR as a mono- rather than multinuclear member of the alkaline phosphatase superfamily.
MCR（移动多粘菌素耐药性）酶催化膦乙醇胺（PEA）向细菌脂 A 添加，威胁到“最后手段”抗生素多粘菌素。分子动力学和密度泛函理论模拟表明，单核锌 MCR 支持 PEA 转移到 Thr285 受体，将 MCR 定位为碱性磷酸酶超家族的单核而不是多核成员。
