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CATH Superfamily 2.60.40.1120

Carboxypeptidase-like, regulatory 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:

"
Carboxypeptidase-like, regulatory 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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

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
Rhamnogalacturonan endolyase. [EC: 4.2.2.23]
Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D- galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non- reducing end.
  • The enzyme is part of the degradation system for rhamnogalacturonan I in Bacillus subtilis strain 168 and Aspergillus aculeatus.
 24 A0A0B0E813 A0A370BN90 A1C995 A1D144 A1D9P9 A2R2L1 A5ABH4 B0XPA2 B0YEH9 B8N5T6
(14 more...)
Metallocarboxypeptidase D. [EC: 3.4.17.22]
Releases C-terminal Arg and Lys from polypeptides.
  • Activated by cobalt.
  • Inhibited by guanidinoethylmercaptosuccinic acid.
  • Belongs to peptidase family M14.
 12 O75976 O75976 O89001 O89001 P42787 P42787 P83852 Q90240 Q90240 Q90240
(2 more...)
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.
 10 A0A384N679 A5A6K7 O17754 P04836 P15087 P16870 P37892 Q00493 Q4R4M3 Q543R4
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
Carboxypeptidase M. [EC: 3.4.17.12]
Cleavage of C-terminal arginine or lysine residues from polypeptides.
  • A membrane-bound enzyme optimally active at neutral pH.
  • Distinct from EC 3.4.17.3 and EC 3.4.17.10.
  • Belongs to peptidase family M14.
 3 P14384 Q5RFD6 Q80V42
Chitinase. [EC: 3.2.1.14]
Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta- linkages in chitin and chitodextrins.
  • The enzyme binds to chitin and randomly cleaves glycosidic linkages in chitin and chitodextrins in a non-processive mode, generating chitooligosaccharides and free ends on which exo-chitinases and exo- chitodextrinases can act.
  • Activity is greatly stimulated in the presence of EC 1.14.99.53, which attacks the crystalline structure of chitin and makes the polymer more accesible to the chitinase.
  • Cf. EC 3.2.1.202.
 2 A5FB63 A5FB63