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
| 3.2.1.10 |
Oligo-1,6-glucosidase.
based on mapping to UniProt P14410
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
-!- This enzyme, like EC 3.2.1.33, can release an alpha-1->6-linked glucose, whereas the shortest chain that can be released by EC 3.2.1.41, EC 3.2.1.142 and EC 3.2.1.68 is maltose. -!- It also hydrolyzes isomaltulose (palatinose), isomaltotriose and panose, but has no action on glycogen or phosphorylase limit dextrin. -!- The enzyme from intestinal mucosa is a single polypeptide chain that also catalyzes the reaction of EC 3.2.1.48. -!- Differs from EC 3.2.1.33 in its preference for short-chain substrates and in its not requiring the 6-glucosylated residue to be at a branch point, i.e. linked at both C-1 and C-4.
|
| 3.2.1.48 |
Sucrose alpha-glucosidase.
based on mapping to UniProt P14410
Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action.
-!- Isolated from intestinal mucosa as a single polypeptide chain also displaying activity toward isomaltose (EC 3.2.1.10).
|
UniProtKB Entries (1)
| P14410 |
SUIS_HUMAN
Homo sapiens
Sucrase-isomaltase, intestinal
|
PDB Structure
| PDB | 3LPP |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.
J.Biol.Chem.
|