Heparan sulfate-glucosamine 3-O-sulfotransferase 1 (HS3ST1)

Heparan sulfate-glucosamine 3-O-sulfotransferase 1 (HS3ST1; also known as 3-OST-1) is an enzyme that catalyzes the transfer of a sulfo group from 3'-phospho-5'-adenylyl sulfate (PAPS) to the 3-O position of a glucosamine residue within heparan sulfate chains, producing a unique sulfation pattern.[1][2][3] This is a critical biosynthetic step in generating heparan sulfate with specific protein binding properties, including high affinity for antithrombin, thereby endowing the polysaccharide with anticoagulant activity[2]. The distinct sulfation patterns generated by HS3ST1 influence cellular processes such as blood coagulation, susceptibility to viral entry (notably herpesviruses with other isoforms), and possibly cancer metastasis due to altered cell surface interactions. The enzyme is one member of a sulfotransferase family, each creating diverse structures for different biological roles. No clinically approved drugs directly target this enzyme, but it is vital in the generation and function of clinically relevant heparan sulfate and heparin.

Other names

Heparan sulfate 3-O-sulfotransferase 13-OST-1HS3ST1

Drugs like heparin depend on the specific sulfation pattern produced by HS3ST1 for high-affinity antithrombin binding and anticoagulant activity[2]. Modulating enzyme activity could indirectly affect susceptibility to infection (e.g., herpes simplex virus)[2]. Inhibition or alteration could disrupt heparan sulfate modifications that are critical for physiological and pathological protein interactions.