D-glucuronyl C5-epimerase (GLCE)

D-glucuronyl C5-epimerase (GLCE) is an enzyme that catalyzes the epimerization of D-glucuronic acid residues to L-iduronic acid residues in maturing heparan sulfate and heparin chains, specifically adjacent to N-sulfate sugar residues[1][2][3][4]. This modification is crucial for the biosynthesis of heparan sulfate glycosaminoglycans, which mediate diverse protein–glycan interactions in development and homeostasis[1][2][3]. GLCE activity shapes the structure of heparan sulfate and heparin, influencing their protein-binding specificity and biological functions[3]. Mutations or altered function of this enzyme are implicated in several developmental syndromes and may play a tumor-suppressive role in certain cancers[1][3]. The enzyme is localized in the Golgi apparatus membrane and functions as a dimer[2][4].

Other names

HSEPIglucuronic acid epimeraseheparan sulfate epimeraseheparosan-N-sulfate-glucuronate 5-epimeraseKIAA0836heparin/heparan sulfate-glucuronic acid C5-epimeraseheparin/heparan sulfate:glucuronic acid C5-epimeraseUDP-glucuronic acid epimeraseglucuronyl C5-epimerase