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 | Cytoplasmic alpha-amylase |
Enzyme Information
| 3.2.1.98 |
Glucan 1,4-alpha-maltohexaosidase.
based on mapping to UniProt P19571
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non- reducing chain ends.
-!- Cf. EC 3.2.1.3, which removes successive glucose residues. -!- Cf. EC 3.2.1.2, which removes successive maltose residues. -!- Cf. EC 3.2.1.116, which removes successive maltotriose residues. -!- Cf. EC 3.2.1.60, which removes successive maltotetraose residues. -!- The products have the alpha-configuration.
|
UniProtKB Entries (1)
| P19571 |
AMT6_BACS7
Bacillus sp. 707
Glucan 1,4-alpha-maltohexaosidase
|
PDB Structure
| PDB | 2GJP |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Bacillus |
| Primary Citation |
Structure of Bacillus halmapalus alpha-amylase crystallized with and without the substrate analogue acarbose and maltose.
Acta Crystallogr.,Sect.F
|
