CATH Classification
Level | CATH Code | Description |
---|---|---|
2 | Mainly Beta | |
2.60 | Sandwich | |
2.60.40 | Immunoglobulin-like | |
2.60.40.1760 | glycosyl hydrolase (family 31) |
Domain Context
CATH Clusters
Superfamily | glycosyl hydrolase (family 31) |
Functional Family | Maltase-glucoamylase, intestinal |
Enzyme Information
3.2.1.20 |
Alpha-glucosidase.
based on mapping to UniProt O43451
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.
|
3.2.1.3 |
Glucan 1,4-alpha-glucosidase.
based on mapping to UniProt O43451
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D- glucose.
-!- Most forms of the enzyme can rapidly hydrolyze 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyze 1,6- and 1,3-alpha-D-glucosidic bonds in other polysaccharides. -!- This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides. -!- EC 3.2.1.20 from mammalian intestine can catalyze similar reactions.
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UniProtKB Entries (1)
O43451 |
MGA_HUMAN
Homo sapiens
Maltase-glucoamylase, intestinal
|
PDB Structure
PDB | 3TOP |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structural insight into substrate specificity of human intestinal maltase-glucoamylase
Protein Cell
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