Cloned (Comment) | Organism |
---|---|
expression of ChGn-1 in mutant sog9 L cells | Mus musculus |
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 | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | required | Mus musculus |
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 | - |
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
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 | Comment | Organism |
---|---|---|
ChGn-1 | - |
Mus musculus |
chondroitin N-acetylgalactosaminyltransferase-1 | - |
Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.8 | - |
assay at | Mus musculus |
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 |