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CATH Superfamily 2.60.220.10

Polysaccharide lyase family 8-like, C-terminal

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Polysaccharide lyase family 8-like, C-terminal
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 1: Chondroitin sulfate ABC exolyase

There are 1 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Chondroitin-sulfate-ABC exolyase. [EC: 4.2.2.21]
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.
 2 C5G6D7 Q8A2I1
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