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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 9: Oligopeptidase A

There are 2 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
Oligopeptidase A. [EC: 3.4.24.70]
Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-Pro-Ala is cleaved, but not Z-(Gly)(5).
  • Differs from thimet oligopeptidase in lack of thiol activation.
  • Belongs to peptidase family M3.
 4946 A0A069XEJ3 A0A069XEJ3 A0A069XEJ3 A0A069XEJ3 A0A069XEJ3 A0A069XEJ3 A0A069XEJ3 A0A069XEJ3 A0A069XEJ3 A0A069XEJ3
(4936 more...)
Peptidyl-dipeptidase Dcp. [EC: 3.4.15.5]
Hydrolysis of unblocked, C-terminal dipeptides from oligopeptides, with broad specificity. Does not hydrolyze bonds in which P1' is Pro, or both P1 and P1' are Gly.
  • Inhibited by captopril, as is peptidyl-dipeptidase A.
  • Belongs to peptidase family M3.
  • Formerly EC 3.4.15.3.
 301 A0A024L2U7 A0A024L2U7 A0A024L2U7 A0A024L2U7 A0A024L2U7 A0A024L2U7 A0A024L2U7 A0A024L2U7 A0A024L2U7 A0A024L2U7
(291 more...)