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大肠杆菌MurG:糖基转移酶超家族的一个范例。

E. Coli MurG: a paradigm for a superfamily of glycosyltransferases.

作者信息

Ha S, Gross B, Walker S

机构信息

Chemistry Department, Princeton University, Princeton, NJ 08544, USA.

出版信息

Curr Drug Targets Infect Disord. 2001 Aug;1(2):201-13. doi: 10.2174/1568005014606116.

Abstract

MurG is an essential bacterial glycosyltransferase that is involved in the biosynthesis of peptidoglycan. The enzyme is found in all organisms that synthesize peptidoglycan and is a target for the design of new antibiotics. A direct assay to study MurG was reported recently, followed shortly by the crystal structure of E. coli MurG. This first MurG structure, combined with sequence data on other glycosyltransferases, has revealed that MurG is a paradigm for a large family of metal ion-independent glycosyltransferases found in both eukaryotes and prokaryotes. A better understanding of MurG could lead to the development of new drugs to combat antibiotic resistant infections, and may also shed light on a broad class of glycosyltransferases.

摘要

MurG是一种必需的细菌糖基转移酶,参与肽聚糖的生物合成。该酶存在于所有合成肽聚糖的生物体中,是新型抗生素设计的靶点。最近报道了一种研究MurG的直接检测方法,随后不久又报道了大肠杆菌MurG的晶体结构。这第一个MurG结构,结合其他糖基转移酶的序列数据,表明MurG是真核生物和原核生物中发现的一大类不依赖金属离子的糖基转移酶的范例。对MurG的更好理解可能会导致开发出对抗抗生素耐药性感染的新药,也可能有助于阐明一类广泛的糖基转移酶。

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