CHST14 transfers SO4(2-) to GalNAc in dermatan or DS

Stable Identifier
Reaction [transition]
Homo sapiens
GalNAc is sulfated on position 4 of GalNAc in dermatan or dermatan sulfate
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Important functional domains in dermatan or dermatan sulfate (DS) are generated by the action of an epimerase (which converts D-glucuronic acid into its epimer L-iduronic acid) together with 4-O-sulfation. These domains are named 4-O-sulfated iduronic acid blocks (Pachebo et al. 2009). Carbohydrate sulfotransferase 14 (CHST14) (Evers et al. 2001) mediates the transfer of sulfate to position 4 of another N-acetylgalactosamine (GalNAc) residue of D2,4(S)2-PG (sulfated on position 2 of IdoA and position 4 of GalNAc) to produce a further sulfated product D2,4,4(S)3-PG (sulfated on another GalNAc in addition to the ones above).

Literature References
PubMed ID Title Journal Year
19661164 Dermatan 4-O-sulfotransferase 1 is pivotal in the formation of iduronic acid blocks in dermatan sulfate

Pacheco, B, Maccarana, M, Malmström, A

Glycobiology 2009
11470797 Molecular cloning and characterization of a dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase

Baenziger, JU, Schachner, M, Kang, HG, Evers, MR, Xia, G

J. Biol. Chem. 2001
Catalyst Activity

N-acetylgalactosamine 4-O-sulfotransferase activity of CHST14 [Golgi membrane]

Orthologous Events
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