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CATH Superfamily 3.40.630.10

Zn peptidases

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:

"
Zn peptidases
".

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 13: carboxypeptidase N catalytic chain

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
Carboxypeptidase E. [EC: 3.4.17.10]
Release of C-terminal arginine or lysine residues from polypeptides.
  • Activated by Co(2+).
  • Inhibited by 1,10-phenanthroline and other chelating agents.
  • pH optimum 5.6.
  • Located in storage granules of secretory cells, and active in processing of protein hormones and bioactive peptides.
  • Distinct from EC 3.4.17.2 and EC 3.4.17.3.
  • Belongs to peptidase family M14.
 13 A0A384N679 A0A384N679 A5A6K7 P04836 P15087 P16870 P16870 P37892 Q00493 Q00493
(3 more...)
Lysine carboxypeptidase. [EC: 3.4.17.3]
Release of a C-terminal basic amino acid, preferentially lysine.
  • Inactivates bradykinin and anaphylatoxins in blood plasma.
  • Belongs to peptidase family M14.
  • Formerly EC 3.4.12.7.
 4 P15169 Q2KJ83 Q9EQV8 Q9JJN5