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
| 3.2.1.176 |
Cellulose 1,4-beta-cellobiosidase (reducing end).
based on mapping to UniProt P0C2S5
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and similar substrates, releasing cellobiose from the reducing ends of the chains.
-!- Some exocellulases, most of which belong to the glycoside hydrolase family 48 (GH48), act at the reducing ends of cellulose and similar substrates. -!- The CelS enzyme from Clostridium thermocellum is the most abundant subunit of the cellulosome formed by the organism. -!- It liberates cellobiose units from the reducing end by hydrolysis of the glycosidic bond, employing an inverting reaction mechanism. -!- Different from EC 3.2.1.91, which attacks cellulose from the non- reducing end.
|
UniProtKB Entries (1)
| P0C2S5 |
GUNS_CLOTM
Hungateiclostridium thermocellum
Cellulose 1,4-beta-cellobiosidase (reducing end) CelS
|
PDB Structure
| PDB | 1L2A |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The crystal structure and catalytic mechanism of cellobiohydrolase CelS, the major enzymatic component of the Clostridium thermocellum Cellulosome.
J.Mol.Biol.
|
