Heparan sulfate-glucosamine 3-O-sulfotransferase 5 (HS3ST5)

Heparan sulfate-glucosamine 3-O-sulfotransferase 5 (HS3ST5) is an enzyme that catalyzes the transfer of a sulfo group from 3′-phosphoadenosine 5′-phosphosulfate (PAPS) to the 3-OH position of glucosamine in heparan sulfate and heparin. This specific 3-O-sulfation creates rare structures in heparan sulfate, notably antithrombin-binding sites essential for its anticoagulant properties and binding sites for herpes simplex virus type 1 entry. HS3ST5 displays broader substrate specificity than other sulfotransferase isoforms, modifying both N-sulfated and N-unsubstituted glucosamine residues adjacent to iduronic acid. It is implicated in several biological and disease processes, including coagulation, viral infection, and possibly cancer. Although there are no approved drugs that target HS3ST5 directly, its central role in heparan sulfate modification makes it a potential target for anticoagulant and antiviral therapeutic strategies[1][2][3][5][6].

Other names

Heparan sulfate glucosamine 3-O-sulfotransferase 5HS3ST53OST5HS3OST53-OST-5h3-OST-5Heparan sulfate 3-O-sulfotransferase 5Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 5NBLA04021heparan sulfate 3-OST-5

Drugs indirectly targeting HS3ST5 would modulate heparan sulfate 3-O-sulfation, affecting: - Formation of antithrombin-binding sites (enhancing or reducing anticoagulant activity) - Formation of viral entry receptors (potential antiviral strategies) - Alteration of cell surface HS composition, impacting protein-ligand interactions