EC Number |
Substrates |
Products |
Reversibility |
---|
2.4.1.226 | more |
further substrates: chondroitin heptaserine, pentaserine, non-sulfated odd-numbered oligosaccharides with a N-acetylgalactosamine residue at the non-reducing terminus except for a trisaccharide |
? |
- |
? |
2.4.1.226 | more |
no substrates: a trisaccharide-serine, an alpha-N-acetylgalactosamine-capped pentasaccharide-serine |
? |
- |
? |
2.4.1.226 | more |
the glucuronic acid transfer rate roughly increases with increasing chain length |
? |
- |
? |
2.4.1.226 | more |
6-O-sulfation of non-reducing terminal N-acetylgalactosamine markedly enhances glucuronic acid transfer |
? |
- |
? |
2.4.1.226 | more |
no substrates: chondroitin, chondroitin sulfate, dermatan sulfate, N-acetylheparosan, hyaluronan, heparan sulfate, heparin, hyaluronan heptasaccharides |
? |
- |
? |
2.4.1.226 | more |
in vitro activity of the recombinant enzyme requires concomitant expression of the chondroitin polymerizing factor ChPF in a fusion protein, mixing of separately expressed proteins does not result in an active complex, overview |
? |
- |
? |
2.4.1.226 | more |
substrate specificities of enzymes CSGlcAT-II and CSS2 in truncated form |
? |
- |
? |
2.4.1.226 | more |
CSGlcA-T exhibits polymerization activity on alpha-thrombomodulin using alpha-thrombomodulin as acceptor incubated with UDP-Gal-NAc and UDP-GlcUA. The chain length of chondroitin formed by the co-expressed proteins ChSy-1,ChSy-2 (CSS3), or ChPF in various combinations is different |
? |
- |
? |
2.4.1.226 | more |
polymerization reactions carried out using alpha-thrombomodulin as an acceptor co-incubated with UDP-GalNAc and UDP-GlcA |
? |
- |
? |
2.4.1.226 | more |
CHSY1, CHSY2 and CHSY3 possess dual, glucuronyltransferase and galactosaminyltransferase enzymatic activities, while the CSGlcA-T acts only by transferring glucuronic acid |
? |
- |
? |