B3GAT dimers transfer 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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B3GAT1 (Kitagawa et al. 1998) and B3GAT2 (Marcos et al. 2002) 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
12522689 Cloning, characterization, and chromosome mapping of the human GlcAT-S gene

Marcos, I, Galán, JJ, Borrego, S, Antiñolo, G

J Hum Genet 2002
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
9506957 Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans

Kitagawa, H, Tone, Y, Tamura, J, Neumann, KW, Ogawa, T, Oka, S, Kawasaki, T, Sugahara, K

J Biol Chem 1998
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
Catalyst Activity

galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity of B3GAT dimers [Golgi membrane]

Orthologous Events
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