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:

"
Glycosidases
".

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 307: Glycogen debranching enzyme

There are 2 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
4-alpha-glucanotransferase. [EC: 2.4.1.25]
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan.
  • An enzymic activity of this nature forms part of the mammalian and Saccharomyces cerevisiae glycogen branching system (see EC 3.2.1.33).
  • Formerly EC 2.4.1.3.
1 P35574
Amylo-alpha-1,6-glucosidase. [EC: 3.2.1.33]
Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin.
  • This enzyme hydrolyzes an unsubstituted glucose unit linked by an alpha(1->6) bond to an alpha(1->4) glucose chain.
  • The enzyme activity found in mammals and Saccharomyces cerevisiae is in a polypeptide chain containing two active centers.
  • The other activity is similar to that of EC 2.4.1.25, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can then hydrolyze.
  • Together, these two activities constitute the glycogen debranching system.
1 P35574
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