CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.980 | Threonyl-tRNA Synthetase; Chain A, domain 2 |
|
3.30.980.50 |
Domain Context
CATH Clusters
| Superfamily | 3.30.980.50 |
| Functional Family |
Enzyme Information
| 3.4.24.3 |
Microbial collagenase.
based on mapping to UniProt Q899Y1
Digestion of native collagen in the triple helical region at Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg at P3'.
-!- Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum. -!- Class I has forms alpha (68 kDa), beta (115 kDa) and gamma (79 kDa); class II has delta (100 kDa), epsilon (110 kDa) and zeta (125 kDa). -!- The two classes are immunologically crossreactive, but have significantly different sequences, and different specificities such that their actions on collagen are complementary. -!- The enzymes also act as peptidyl-tripeptidases. -!- Variants of the enzyme have been purified from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio, Vibrio B-30 (ATCC 21250) and V.alginolyticus (previously Achromobacter iophagus). -!- Also known from Streptomyces sp. -!- Belongs to peptidase family M9. -!- Formerly EC 3.4.4.19, EC 3.4.24.8 and EC 3.4.99.5.
|
UniProtKB Entries (1)
| Q899Y1 |
COLT_CLOTE
Clostridium tetani E88
Collagenase ColT
|
PDB Structure
| PDB | 4AR8 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural Basis for Activity Regulation and Substrate Preference of Clostridial Collagenases G, H, and T.
J.Biol.Chem.
|
