ENZYME entry: EC 3.4.24.3
| Accepted Name |
|---|
| Microbial collagenase.
|
| Alternative Name(s) |
|---|
| Clostridiopeptidase A. |
| Clostridium histolyticum collagenase. |
| Collagenase A. |
| Collagenase I. |
| Reaction catalysed |
|---|
| 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' |
| Cofactor(s) |
|---|
| Zn(2+).
|
| Comment(s) |
|---|
- 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.
|
| Cross-references |
|---|
| BRENDA | 3.4.24.3 |
| EC2PDB | 3.4.24.3 |
| ExplorEnz | 3.4.24.3 |
| PRIAM enzyme-specific profiles | 3.4.24.3 |
| KEGG Ligand Database for Enzyme Nomenclature | 3.4.24.3 |
| IUBMB Enzyme Nomenclature | 3.4.24.3 |
| IntEnz | 3.4.24.3 |
| MEDLINE | Find literature relating to 3.4.24.3 |
| MetaCyc | 3.4.24.3 |
| UniProtKB/Swiss-Prot |
|
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