CHSY1 transfers GalNAc to chondroitin

Stable Identifier
R-HSA-9632033
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
GalNAc is added to chondroitin
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

An N-acetylgalactosamine (GalNAc) moiety is added to the chondroitin chain by dual-activity enzymes, the chondroitin sulfate synthases 1-3 (CHSY1, CHPF and CHSY3 respectively) (Kitagawa et al. 2001, Yada et al. 2003, Yada et al. 2003b). They possess both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity, the latter activity used in this reaction. These three enzymes require divalent metals as cofactors, manganese producing the highest activities. The repeated disaccharide units of GlcA-GalNAc identify this glycosaminoglycan as chondroitin.

Literature References
PubMed ID Title Journal Year
12761225 Chondroitin sulfate synthase-2. Molecular cloning and characterization of a novel human glycosyltransferase homologous to chondroitin sulfate glucuronyltransferase, which has dual enzymatic activities

Yada, T, Gotoh, M, Sato, T, Shionyu, M, Go, M, Kaseyama, H, Iwasaki, H, Kikuchi, N, Kwon, YD, Togayachi, A, Kudo, T, Watanabe, H, Narimatsu, H, Kimata, K

J Biol Chem 2003
11514575 Molecular cloning and expression of a human chondroitin synthase

Kitagawa, H, Uyama, T, Sugahara, K

J Biol Chem 2001
12907687 Chondroitin sulfate synthase-3. Molecular cloning and characterization

Yada, T, Sato, T, Kaseyama, H, Gotoh, M, Iwasaki, H, Kikuchi, N, Kwon, YD, Togayachi, A, Kudo, T, Watanabe, H, Narimatsu, H, Kimata, K

J Biol Chem 2003
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity of CHSY1 [Golgi membrane]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created