Reactome | B3GAT dimers transfer GlcA to tetrasaccharide linker

B3GAT dimers transfer GlcA to tetrasaccharide linker

Stable Identifier

R-HSA-1889955

Type

Reaction [transition]

Species

Homo sapiens

Compartment

Golgi membrane, Golgi lumen

Synonyms

A glucuronate moiety is the fourth addition to the tetrasaccharide linker

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B3GAT dimers transfer GlcA to 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