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CATH Superfamily 2.140.10.30

Dipeptidylpeptidase IV, N-terminal domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was: waiting to be named.

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 11491: Dipeptidyl peptidase IV

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
Dipeptidyl-peptidase IV. [EC: 3.4.14.5]
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.
  • A membrane-bound serine-type peptidase in mammals.
  • EC 3.4.14.11 catalyzes a similar reaction.
  • Belongs to peptidase family S9B.
 14 A0A099KAV2 A0A099KAV2 A0A099KLZ8 A0A099KLZ8 A0A0K2J4F0 A0A0K2J4F0 A0A134DP81 A0A134DP81 Q0C2V8 Q0C2V8
(4 more...)
Xaa-Xaa-Pro tripeptidyl-peptidase. [EC: 3.4.14.12]
Hydrolysis of Xaa-Xaa-Pro-|-Yaa- releasing the N-terminal tripeptide of a peptide with Pro as the third residue (position P1) and where Yaa is not proline.
  • This cell-surface-associated serine exopeptidase is found in the Gram-negative, anaerobic bacterium Porphyromonas gingivalis, which has been implicated in adult periodontal disease.
  • The enzyme releases tripeptides from the free amino terminus of peptides and small proteins, such as interleukin-6.
  • The enzyme possesses an absolute requirement for a proline residue at the P1 position but is completely inactivated by a proline residue at the P1' position.
  • The size of the peptide does not affect the rate of reaction.
 8 A0A0K2J4F0 A0A0K2J4F0 A0A134DP81 A0A134DP81 B2RJX3 B2RJX3 Q7MUW6 Q7MUW6