摘要
UDP-葡萄糖是所有生物中多种细胞生理过程的重要代谢物。在原核生物中,它参与了海藻糖(一种渗透保护剂)的合成,通过Leloir通路参与半乳糖利用,在细菌包膜的组件合成中发挥重要作用,尤其是代表细菌病原体必需毒力因子的脂多糖及其包膜。UDP-葡萄糖在细菌中通过原核UDP-葡萄糖焦磷酸化酶 (UGP,EC 2.7.7.9,一种属于糖的酶:核苷酸转移酶) 而合成。尽管UGP活性普遍分布于生命的所有领域,原核UGPs在进化上与其真核相对物无关。总的来说,这些特征使得细菌UGP成为一个具有吸引力的候选靶标用于新一代抗生素的发现和发展。本文综述了细菌UGPs结构和功能的目前知识及其作为候选药物靶标的潜能。
关键词: 抗生素,药物发现,药物靶标,GalU,糖生物学,糖基转移酶,UGP。
Current Medicinal Chemistry
Title:Structure and Function of Prokaryotic UDP-Glucose Pyrophosphorylase, A Drug Target Candidate
Volume: 22 Issue: 14
Author(s): M. Alvaro Berbis, Jose Maria Sanchez-Puelles, F. Javier Canada and Jesus Jimenez-Barbero
Affiliation:
关键词: 抗生素,药物发现,药物靶标,GalU,糖生物学,糖基转移酶,UGP。
摘要: UDP-glucose is an essential metabolite for a variety of processes in the cell physiology in all organisms. In prokaryotes, it is involved in the synthesis of trehalose, an osmoprotectant, in galactose utilization via the Leloir pathway and it plays a key role in the synthesis of the components of the bacterial envelope, particularly the lipopolysaccharide and the capsule, which represent necessary virulence factors of many bacterial pathogens. UDP-glucose is synthesized in bacteria by the prokaryotic UDP-glucose pyrophosphorylase (UGP, EC 2.7.7.9), an enzyme belonging to the family of sugar:nucleotidyl transferases. Despite the ubiquitous distribution of UGP activity in all domains of life, prokaryotic UGPs are evolutionarily unrelated to their eukaryotic counterparts. Taken together, these features make of bacterial UGP an attractive target candidate for the discovery and development of new generation antibiotics. This review summarizes the current knowledge on structure and function of bacterial UGPs, underlying their potential as drug target candidates.
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Cite this article as:
M. Alvaro Berbis, Jose Maria Sanchez-Puelles, F. Javier Canada and Jesus Jimenez-Barbero , Structure and Function of Prokaryotic UDP-Glucose Pyrophosphorylase, A Drug Target Candidate, Current Medicinal Chemistry 2015; 22 (14) . https://dx.doi.org/10.2174/0929867322666150114151248
DOI https://dx.doi.org/10.2174/0929867322666150114151248 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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