CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.400 | Oligo-1,6-glucosidase; domain 2 |
|
3.90.400.10 | Oligo-1,6-glucosidase; Domain 2 |
Domain Context
CATH Clusters
| Superfamily | Oligo-1,6-glucosidase; Domain 2 |
| Functional Family | Sucrose isomerase |
Enzyme Information
| 3.2.1.10 |
Oligo-1,6-glucosidase.
based on mapping to UniProt P21332
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.
|
UniProtKB Entries (1)
| P21332 |
O16G_BACCE
Bacillus cereus
Oligo-1,6-glucosidase
|
PDB Structure
| PDB | 1UOK |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A resolution: structural characterization of proline-substitution sites for protein thermostabilization.
J.Mol.Biol.
|