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CATH Superfamily 3.40.390.10

Collagenase (Catalytic Domain)

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Collagenase (Catalytic Domain)
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 7: Collagenase 3

There are 6 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Interstitial collagenase. [EC: 3.4.24.7]
Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.
  • The enzyme takes its name from substrates of the interstitial collagen group - types I, II and III, all of which are cleaved in the helical domain.
  • Alpha-macroglobulins are cleaved much more rapidly.
  • The enzyme is widely distributed in vertebrate animals.
  • Belongs to peptidase family M10B.
 9 C9VZX3 C9VZX3 P03956 P21692 P21692 P28053 Q9EPL5 Q9EPL6 Q9XSZ5
Stromelysin 2. [EC: 3.4.24.22]
Similar to stromelysin 1, but action on collagen types III, IV and V is weak.
  • Digests gelatin types I, III, IV, V, fibronectin and proteoglycan.
  • Belongs to peptidase family M10B.
 6 A1L3D0 A1L3D0 O55123 O55123 P07152 P09238
Stromelysin 1. [EC: 3.4.24.17]
Preferential cleavage where P1', P2' and P3' are hydrophobic residues.
  • Extracellular endopeptidase of vertebrate tissues.
  • Degradation of proteoglycans, fibronectin, collagen type III, IV, V and IX and activates procollagenase.
  • Belongs to peptidase family M10B.
 5 P03957 P08254 P28862 Q28397 Q6Y4Q5
Matrilysin. [EC: 3.4.24.23]
Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha-2(I) > alpha-1(I).
  • Similar in specificity to stromelysin, but more active on azocoll.
  • Belongs to peptidase family M10B.
 4 P09237 P50280 P55032 Q10738
Neutrophil collagenase. [EC: 3.4.24.34]
Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.
  • Similar to interstitial collagenase in specificity.
  • Stored in the specific granules of neutrophil leukocytes.
  • Belongs to peptidase family M10B.
 3 O70138 O88766 P22894
Macrophage elastase. [EC: 3.4.24.65]
Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin.
  • Belongs to peptidase family M10B.
 3 P34960 P39900 Q63341
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