CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.80 | Glycosidases |
Domain Context
CATH Clusters
| Superfamily | Glycosidases |
| 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.
|
UniProtKB Entries (1)
| O43451 |
MGA_HUMAN
Homo sapiens
Maltase-glucoamylase, intestinal
|
PDB Structure
| PDB | 2QMJ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Drosophila |
| Primary Citation |
Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity
J.Mol.Biol.
|
