CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.50 | Alpha/alpha barrel |
|
1.50.10 | Glycosyltransferase |
|
1.50.10.10 |
Domain Context
CATH Clusters
| Superfamily | 1.50.10.10 |
| Functional Family |
Enzyme Information
| 3.2.1.3 |
Glucan 1,4-alpha-glucosidase.
based on mapping to UniProt P08017
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)
| P08017 |
AMYG_SACFI
Saccharomycopsis fibuligera
Glucoamylase GLU1
|
PDB Structure
| PDB | 2F6D |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of the complex of a yeast glucoamylase with acarbose reveals the presence of a raw starch binding site on the catalytic domain.
Febs J.
|