B3GAT dimers transfer GlcA to tetrasaccharide linker

Stable Identifier
Reaction [transition]
Homo sapiens
A glucuronate moiety is the fourth addition to the tetrasaccharide linker
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
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
10842173 Structure/function of the human Ga1beta1,3-glucuronosyltransferase. Dimerization and functional activity are mediated by two crucial cysteine residues

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

J Biol Chem 2000
12522689 Cloning, characterization, and chromosome mapping of the human GlcAT-S gene

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

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

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

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

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

J Biol Chem 2004
Catalyst Activity

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

Orthologous Events
Cite Us!