The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_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 52734: Trehalose synthase (Maltose alpha-D-glucosyltransf...

There are 5 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
Maltose alpha-D-glucosyltransferase. [EC: 5.4.99.16]
Maltose = alpha,alpha-trehalose.
    812 A0A017HHL3 A0A017HHL3 A0A024H6Q9 A0A024H6Q9 A0A045HSE3 A0A045HSE3 A0A049DQL3 A0A049DQL3 A0A058YG91 A0A058YG91
    (802 more...)
    Alpha-amylase. [EC: 3.2.1.1]
    Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
    • Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration.
    • The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.
    406 A0A010YYC5 A0A010YYC5 A0A011P0B3 A0A011P0B3 A0A011PXW6 A0A011PXW6 A0A011QI48 A0A011QI48 A0A021VUN6 A0A021VUN6
    (396 more...)
    Alpha-glucosidase. [EC: 3.2.1.20]
    Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.
    • Group of enzymes whose specificity is directed mainly toward the exohydrolysis of 1,4-alpha-glucosidic linkages, and that hydrolyze oligosaccharides rapidly, relative to polysaccharides, which are hydrolyzed relatively slowly, or not at all.
    • The intestinal enzyme also hydrolyzes polysaccharides, catalyzing the reactions of EC 3.2.1.3, and, more slowly, hydrolyzes 1,6-alpha-D- glucose links.
    4 A0A073CL45 A0A073CL45 Q1YG23 Q1YG23
    Maltokinase. [EC: 2.7.1.175]
    ATP + maltose = ADP + alpha-maltose 1-phosphate.
    • Formerly EC 2.7.1.n8.
    2 Q88FN0 Q88FN0
    Glucan 1,6-alpha-glucosidase. [EC: 3.2.1.70]
    Hydrolysis of (1->6)-alpha-D-glucosidic linkages in (1->6)-alpha-D- glucans and derived oligosaccharides.
    • Hydrolysis is accompanied by inversion at C-1, so that new reducing ends are released in the beta-configuration.
    • Dextrans and isomaltosaccharides are hydrolyzed, as is isomaltose, but very slowly.
    • The enzyme from some sources also possesses the activity of EC 3.2.1.59.
    2 A0A0T8KVF2 A0A0T8KVF2
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