CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.50 | Alpha/alpha barrel |
|
1.50.10 | Glycosyltransferase |
|
1.50.10.100 | Chondroitin AC/alginate lyase |
Domain Context
CATH Clusters
| Superfamily | Chondroitin AC/alginate lyase |
| Functional Family |
Enzyme Information
| 4.2.2.21 |
Chondroitin-sulfate-ABC exolyase.
based on mapping to UniProt C5G6D7
Exolytic removal of Delta(4)-unsaturated disaccharide residues from the non-reducing ends of both polymeric chondroitin/dermatan sulfates and their oligosaccharide fragments.
-!- Degrades a variety of glycosaminoglycans of the chondroitin-sulfate- and dermatan-sulfate type. -!- Chondroitin sulfate, chondroitin-sulfate proteoglycan and dermatan sulfate are the best substrates but the enzyme can also act on hyaluronan at a much lower rate. -!- The related enzyme EC 4.2.2.20 has the same substrate specificity but produces a mixture of oligosaccharides of different sizes that are ultimately degraded to tetra- and disaccharides. -!- Both enzymes act by the removal of a relatively acidic C-5 proton of the uronic acid followed by the elimination of a 4-linked hexosamine, resulting in the formation of an unsaturated C4-C5 bond on the hexuronic acid moiety of the products. -!- Formerly EC 4.2.2.4 and EC 4.2.99.6.
|
UniProtKB Entries (1)
| C5G6D7 |
CABC2_BACT4
Bacteroides thetaiotaomicron
Chondroitin sulfate ABC exolyase
|
PDB Structure
| PDB | 2Q1F |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Composite active site of chondroitin lyase ABC accepting both epimers of uronic acid.
Glycobiology
|
