<![CDATA[The escalating threat of antimicrobial resistance (AMR) has emerged as a pressing global health challenge, with Gram-negative organisms most notably Escherichia coli bearing substantial responsibility for its clinical impact. This review critically assesses the feasibility of targeting UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) as an antibacterial drug target and the pharmacological potential of xanthorrhizol. The latter compound represents the predominant bioactive constituent isolated from the rhizome of Curcuma xanthorrhiza, a plant with established medicinal application. This review describes the robust antimicrobial spectrum of xanthorrhizol and defines the structural arrangements of the MurB enzyme that allow its pharmacological inhibition, through a thorough and exhaustive assessment of published literature. Central to our findings is the observation that MurB occupies an indispensable position within the peptidoglycan assembly pathway of bacteria, a function for which no mammalian counterpart exists an attribute that underscores its exceptional suitability as a selective therapeutic target, providing for a highly selective targeting mechanism with little risk of toxicity to the host. Xanthorrhizol also showed potent bactericidal activity against Gram-negative bacteria by successfully attacking their cellular defenses, preventing biofilm formation, and significantly reducing the count of viable cells. Therefore, xanthorrhizol looks like a very rational candidate for the development of new drugs. In conclusion, xanthorrhizol as an inhibitor of the MurB enzyme is a promising novel strategy in the fight against resistant E. coli infections and provides a good theoretical basis that needs further molecular docking simulations and in vitro validation.]]>
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