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β(1,3)-D-glucan synthase is a membrane-bound enzyme complex responsible for synthesizing (1,3)-β-D-glucan, a major structural polysaccharide in the fungal cell wall. This enzyme is essential for fungal viability and serves as a key pharmacological target for antifungal drugs such as echinocandins (e.g., caspofungin, anidulafungin, micafungin) and ibrexafungerp. It catalyzes the polymerization of UDP-glucose to form linear (1,3)-β-D-glucan chains. The product forms the primary scaffold of the fungal cell wall and is critical for maintaining cell shape and integrity. Inhibition of β(1,3)-D-glucan synthase disrupts fungal cell wall synthesis leading to osmotic instability and ultimately cell death—making it an effective antifungal drug target. Resistance can arise via mutations in FKS genes encoding its catalytic subunits. Found widely among fungi including pathogenic species (Candida, Aspergillus, Cryptococcus, Pneumocystis) but absent from mammalian cells—contributing to its value as an antifungal target.
Inhibition of β(1,3)-D-glucan synthase, disrupting fungal cell wall synthesis
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