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作 者:Marcelo Monteiro Pedroso David W.Waite Okke Melse Liam Wilson Natasa Mitic Ross P.McGeary Iris Antes Luke W.Guddat Philip Hugenholtz Gerhard Schenk
机构地区:[1]School of Chemistry and Molecular Biosciences,The University of Queensland,St.Lucia,QLD,Brisbane 4072,Australia [2]Australian Centre for Ecogenomics,The University of Queensland,St.Lucia,QLD,Brisbane 4072,Australia [3]Center for Integrated Protein Science Munich at the TUM School of Life Sciences,Technische Universit(a)t München,85354 Freising,Germany [4]Department of Chemistry,Maynooth University,Maynooth,Co.Kildare,Ireland
出 处:《Protein & Cell》2020年第8期613-617,共5页蛋白质与细胞(英文版)
摘 要:Dear Editor, Antibiotic resistance has emerged as a major threat to global health;multi-drug resistant bacteria already kill more patients in the United States each year than HIV/AIDS, Parkinson's disease, emphysema and homicide combined (Laxminarayan et al., 2013).Among the most effective bacterial resistance mechanisms are β-lactamases, a family of enzymes that are divided into four distinct classes.Classes A, C and D (serine-β-lactamases, SBLs) use a catalytic site serine residue to initiate inactivation of the antibiotic, while Class B (metallo-β-lactamases, MBLs) relies on a Zn2+-activated hydroxide (Walsh et al., 2005;Bush and Jacoby,2010;Mitic et al., 2014;Lisa et al., 2017).Clinically relevant inhibitors of Class C and D SBLs are available and in use (e.g., clavulanic acid (CA), Drawz et al., 2010), but for MBLs the search for such inhibitors has remained challenging (McGeary et al., 2017).
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