Reaction: B3GALNT2 transfers GalNAc to GlcNAc-Man-DAG1

- in pathway: O-linked glycosylation
Three enzymes are involved in the biosynthesis of a phosphorylated O-mannosyl trisaccharide structure (N-acetylgalactosamine-beta-1,3-N-acetylglucosamine-beta-1,4-(phosphate-6-)mannose) present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Defects in any of these enzymes can lead to congenital muscular dystrophy.

The second step is catalysed by UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2 (B3GALNT2), an ER membrane-associated enzyme that transfers N-acetylgalactosamine (GalNAc) to GlcNAc-Man-DAG1 via a 1-3 glycosidic bond (Hiruma et al. 2004, Yoshida-Moriguchi et al. 2013). Defects in B3GALNT2 can cause muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A11 (MDDGA11), a hypoglycosylation defect resulting in a reduced ability of DAG1 to bind laminin and other extracellular matrix ligands. The disorder is characterised by dystroglycanopathy with muscle and brain anomolies (Stevens et al. 2013).
Reaction - small molecule participants:
UDP [endoplasmic reticulum lumen]
UDP-GalNAc [endoplasmic reticulum lumen]
Reactome.org reaction link: R-HSA-8931648

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Reaction input - small molecules:
UDP-N-acetyl-D-galactosamine(2-)
ChEBI:57847
Reaction output - small molecules:
UDP
ChEBI:17659
Reactome.org link: R-HSA-8931648