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Literature summary for 2.4.1.174 extracted from

  • Izumikawa, T.; Koike, T.; Kitagawa, H.
    Chondroitin 4-O-sulfotransferase-2 regulates the number of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1 (2012), Biochem. J., 441, 697-705.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of ChGn-1 in mutant sog9 L cells Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information construction of L-shRNA ChGn-1-1 and L-shRNA ChGn-1-2 transfected L cells, and analysis of chondroitin sulfate chain lengths. The silencing of the genes results in a 60-80% reduction in steady-state ChGn-1 mRNA and an 18-22% decrease in CS when compared with control L cells. Overexpression of ChGn-1 slightly increases CS levels in L cells Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus in vitro chondroitin polymerization does not occur on the non-reducing terminal GalNAc-linkage pentasaccharide structure ?
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan Mus musculus
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UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information in vitro chondroitin polymerization does not occur on the non-reducing terminal GalNAc-linkage pentasaccharide structure Mus musculus ?
-
?
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
ChGn-1
-
Mus musculus
chondroitin N-acetylgalactosaminyltransferase-1
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Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.8
-
assay at Mus musculus

General Information

General Information Comment Organism
malfunction deficiency in chondroitin N-acetylgalactosaminyltransferase-1 reduces the numbers of chondroitin sulfate chains, leading to skeletal dysplasias in mice. Knockdown of ChGn-1 decreases chondroitin sulfate levels in L cells, chondroitin sulfate chain lengths in L-shRNAChGn-1-1, L-shRNA ChGn-1-2, and mock-transfected murine L cells, overview Mus musculus
physiological function ChGn-1 initiates chondroitin sulfate biosynthesis by transferring the first N-acetylgalactosamine to the tetrasaccharide in the protein linkage region of chondroitin sulfate, overview. c-2 efficiently transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate to position 4 of non-reducing terminal GalNAc-linkage residues, and the number of chondroitin chains is regulated by the expression levels of C4ST-2 and of ChGn-1. C4ST-2 plays a key role in regulating levels of chondroitin sulfate synthesized via ChGn-1, overview Mus musculus