原核UDP-葡萄糖焦磷酸化酶的结构和功能，一个候选的药物靶标

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.

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