Reactome | B3GAT3 dimer transfers GlcA to tetrasaccharide linker

B3GAT3 dimer transfers GlcA to tetrasaccharide linker

Stable Identifier

R-HSA-9638064

Type

Reaction [transition]

Species

Homo sapiens

Compartment

Golgi membrane, Golgi lumen

Synonyms

A glucuronate moiety is the fourth addition to the tetrasaccharide linker

ReviewStatus

5/5

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B3GAT3 dimer transfers GlcA to 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
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
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