UDP-xylose 4-epimerase (UXE)

UDP-xylose 4-epimerase (UXE), also known as UDP-L-arabinose 4-epimerase, is an enzyme that catalyzes the reversible interconversion of UDP-D-xylose and UDP-L-arabinose [1, 3, 5]. This enzyme is primarily found in plants, fungi, and certain bacteria, where it plays a critical role in the biosynthesis of cell wall polysaccharides and extracellular glycans [5, 6, 30]. In plants, it provides the UDP-L-arabinose required for the synthesis of pectins and hemicelluloses, while in pathogenic microorganisms, it is involved in the production of surface polysaccharides essential for biofilm formation and virulence [1, 3, 11]. Because UXE is not present in humans, it is considered a promising target for the development of novel anti-infective agents, particularly against antibiotic-resistant bacteria and pathogenic fungi [1, 11]. Inhibition of this enzyme can disrupt the structural integrity of the pathogen or reduce its ability to form protective biofilms, thereby enhancing the host's immune response or the efficacy of co-administered treatments [3, 11]. Current research efforts are focused on identifying selective small-molecule inhibitors that can distinguish between the pathogen's UXE and human UDP-sugar epimerases, such as UDP-glucose 4-epimerase (GALE), to minimize potential off-target effects [4, 11].

Other names

UDP-L-arabinose 4-epimeraseUridine diphosphate xylose 4-epimeraseUXE1ARA1Uxe

Inhibition of the interconversion between UDP-xylose and UDP-arabinose, which disrupts the synthesis of essential cell wall or surface polysaccharides in pathogens [1, 11].