Beta-1,3-D-glucan synthase

Beta-1,3-D-glucan synthase is a multi-subunit enzyme complex and a member of the glycosyltransferase superfamily, primarily responsible for the synthesis of beta-1,3-D-glucan, a critical scaffold component of the fungal cell wall. The main catalytic subunit in many fungi is FKS1, which catalyzes the transfer of glucose from UDP-glucose to elongate the beta-1,3-D-glucan polymer, forming the backbone for cross-linked cell wall structures. The enzyme is embedded in the plasma membrane and its activity is unique to fungi, making it a prime target for antifungal agents such as echinocandins and ibrexafungerp. Loss or inhibition of this enzyme disrupts cell wall integrity, leading to osmotic fragility and cell death. The structure of the enzyme includes a conserved glycosyltransferase domain and multiple transmembrane helices, with the regulatory protein Rho1 playing a role in its activation. Resistance to inhibitors is most commonly associated with mutations in the FKS1 gene[1][2][3][5][6].

Other names

1,3-beta-glucan synthaseβ-1,3-glucan synthaseBeta-1,3-glucan synthase1,3-β-D-glucan synthaseCallose synthaseFKS1 (in yeast; refers to the main catalytic subunit)

Inhibition of (beta)-1,3-D-glucan synthesis in fungal cell walls, leading to cell lysis and death