B3GAT dimers transfer GlcA to tetrasaccharide linker
Gal-Gal-Xyl-proteins + UDP-GlcA → UDP + GlcA-Gal-Gal-Xyl-proteins + H+
- Reactome
- R-HSA-1889955
- Compartment
- Golgi membrane · Golgi lumen
- Rhea
- RHEA:24169
Inputs
- Gal-Gal-Xyl-proteinsR-HSA-2064214, Golgi lumen
- UDP-GlcACHEBI:58052, C15H19N2O18P2, Golgi lumen
Outputs
- UDPCHEBI:58223, C9H11N2O12P2, Golgi lumen
- GlcA-Gal-Gal-Xyl-proteinsR-HSA-2064225, Golgi lumen
- H+CHEBI:15378, H, Golgi lumen
Catalysed by
- galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity of B3GAT dimers [Golgi membrane]EC 2.4.1.135
Literature
- Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1 J Biol Chem, 2004
- Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans J Biol Chem, 1998
- Structure/function of the human Ga1beta1,3-glucuronosyltransferase. Dimerization and functional activity are mediated by two crucial cysteine residues J Biol Chem, 2000
- Cloning, characterization, and chromosome mapping of the human GlcAT-S gene J Hum Genet, 2002