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 220.127.116.11), 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.
Keywords: Antibiotic, drug discovery, drug target, GalU, glycobiology, glycosyltransferase, UGP.
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