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 | Acidic endochitinase SE2 |
Enzyme Information
| 3.2.1.14 |
Chitinase.
based on mapping to UniProt P23472
Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta- linkages in chitin and chitodextrins.
-!- The enzyme binds to chitin and randomly cleaves glycosidic linkages in chitin and chitodextrins in a non-processive mode, generating chitooligosaccharides and free ends on which exo-chitinases and exo- chitodextrinases can act. -!- Activity is greatly stimulated in the presence of EC 1.14.99.53, which attacks the crystalline structure of chitin and makes the polymer more accesible to the chitinase. -!- Cf. EC 3.2.1.202.
|
| 3.2.1.17 |
Lysozyme.
based on mapping to UniProt P23472
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl- D-glucosamine residues in chitodextrins.
-!- Cf. EC 3.2.1.14.
|
UniProtKB Entries (1)
| P23472 |
CHLY_HEVBR
Hevea brasiliensis
Hevamine-A
|
PDB Structure
| PDB | 1LLO |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis.
Biochemistry
|
