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Literature summary for 2.4.1.174 extracted from

  • Ogawa, H.; Hatano, S.; Sugiura, N.; Nagai, N.; Sato, T.; Shimizu, K.; Kimata, K.; Narimatsu, H.; Watanabe, H.
    Chondroitin sulfate synthase-2 is necessary for chain extension of chondroitin sulfate but not critical for skeletal development (2012), PLoS ONE, 7, e43806.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.174

Cloned(Commentary)

Cloned (Comment) Organism
CSS1 quantitative expression analysis by realtime RT-PCR, overview Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information downregulation of CSS1 by siRNA Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan Mus musculus
-
 UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Mus musculus
-
cartilage
-
 Mus musculus
-
cell culture
-
 Mus musculus
-
chondrocyte
-
 Mus musculus
-
heart
-
 Mus musculus
-
kidney
-
 Mus musculus
-
liver
-
 Mus musculus
-
lung
-
 Mus musculus
-
additional information CSS1 quantitative tissue expression analysis by realtime RT-PCR, overview Mus musculus
-
skin
-
 Mus musculus
-
small intestine
-
 Mus musculus
-
spleen
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
-
 Mus musculus UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
 ?

Synonyms

Synonyms Comment Organism
chondroitin sulfate synthase-1
-
 Mus musculus
CSS1
-
 Mus musculus

General Information

General Information Comment Organism
malfunction CSS2 knockout chondrocyte culture systems, together with siRNA of CSS1, reveal the presence of two CS chain species in length, suggesting two steps of CS chain polymerization; i.e., elongation from the linkage region up to Mr of about 10000 and further extension Mus musculus
metabolism CSS1 and CSS2 differently contribute to chondroitin sulfate biosynthesis, mechanism of chondroitin sulfate biosynthesis, overview. CSS1 participates in both the chondroitin sulfate chain initiation and polymerization, and CSS2 participates in the polymerization, especially in further extension Mus musculus
additional information the enzyme occurs in a heterooligomer complex, chondroitin sulfate synthase-1 (CSS1)/chondroitin synthase-1 Mus musculus