B3GAT3 dimer transfers GlcA to tetrasaccharide linker

Stable Identifier
Reaction [transition]
Homo sapiens
A glucuronate moiety is the fourth addition to the tetrasaccharide linker
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Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 (B3GAT3) (Ouzzine et al. 2000) transfer a glucuronate (GlcA) residue via a beta1,3-linkage to a terminal galactose. The B3GATs are homodimeric and require manganese as a cofactor (Kakuda et al. 2004, Ouzzine et al. 2000). The tetrasaccharide linker is now complete, ready to accept further hexosamine additions. The type of hexosamine added is critical in determining which glycosaminoglycan (GAG) is formed.

Literature References
PubMed ID Title Journal Year
14993226 Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1

Kakuda, S, Shiba, T, Ishiguro, M, Tagawa, H, Oka, S, Kajihara, Y, Kawasaki, T, Wakatsuki, S, Kato, R

J Biol Chem 2004
10842173 Structure/function of the human Ga1beta1,3-glucuronosyltransferase. Dimerization and functional activity are mediated by two crucial cysteine residues

Ouzzine, M, Gulberti, S, Netter, P, Magdalou, J, Fournel-Gigleux, S

J Biol Chem 2000
Catalyst Activity

galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity of B3GAT3:Mn2+ dimer [Golgi membrane]

Orthologous Events
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