The addition of GalNAc to the terminal glucuronate residue forms chondroitin

Stable Identifier
Reaction [transition]
Homo sapiens
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Chondroitin sulfate N-acetylgalactosaminyltransferases 1 and 2 (CSGALNACT1 and 2) (Uyama et al. 2002, Gotoh et al. 2002) transfer N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the glucuronate (GlcA) residue of the linker sequence. This first addition to the linker determines this GAG to be chondroitin. Chondroitin is comprised of the repeating disaccharide unit GalNAc-GlcA.
Literature References
PubMed ID Title Journal Year
11788602 Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase: the key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate

Uyama, T, Kitagawa, H, Sugahara, K, Tamura Ji, J

J Biol Chem 2002
12163485 Enzymatic synthesis of chondroitin with a novel chondroitin sulfate N-acetylgalactosaminyltransferase that transfers N-acetylgalactosamine to glucuronic acid in initiation and elongation of chondroitin sulfate synthesis

Yada, T, Kwon, YD, Kudo, T, Iwasaki, H, Gotoh, M, Watanabe, H, Togayachi, A, Kameyama, A, Kimata, K, Inaba, N, Sato, T, Mochizuki, H, Narimatsu, H, Nishihara, S, Kikuchi, N, Akashima, T, Zhang, Y

J Biol Chem 2002
Catalyst Activity

glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity of CSGALNACT [Golgi membrane]

Orthologous Events
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