Identification and characterization of the functional tetrameric UDP-glucose pyrophosphorylase from <i>Klebsiella pneumoniae</i>.

ABSTRACT: In all kingdoms of life, the enzyme uridine diphosphate-glucose pyrophosphorylase (UGP) occupies a central role in metabolism, as its reaction product uridine diphosphate-glucose (UDP-Glc) is involved in various crucial cellular processes. Pathogens, including fungi, parasites, and bacteria, depend on UGP for the synthesis of virulence factors; in particular, various bacterial species utilize UDP-Glc and its derivatives for the synthesis of lipopolysaccharides, capsular polysaccharides, and biofilm exopolysaccharides. UGPs have, therefore, gained attention as anti-bacterial drug target candidates, prompting us to study their structure-function relationships to provide a basis for the rational development of specific inhibitors. UGP function is tied to its oligomeric state, and the majority

SUBMITTER: Ramon Roth I 

PROVIDER: S-EPMC11796359 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature