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CATH Superfamily 3.40.50.1820

Alpha/Beta hydrolase fold, catalytic 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 115767: Peptidase, family S9, prolyl oligopeptidase

There are 3 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
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 A0A0D5BJJ2 A0A0S2HWV0 A0A143PFV5 A0A199XT43 A0A1A7KKZ9 A0A1B2U0U3 A0A1E7V1R6 A0A1E7WN14
Acylaminoacyl-peptidase. [EC: 3.4.19.1]
Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.
  • Best if P1 = Ser, Ala, Met; poor if P1 = Gly, Tyr, Asp, Asn or Pro.
  • Group of similar enzymes liberating N-acetyl or N-formyl amino acid from proteins and peptides.
  • Active at neutral pH.
  • Several variants of this enzyme exist; the human erythrocyte enzyme is relatively specific for removal of N-acetylalanine from peptides.
  • Display dipeptidyl-peptidase activity on glycyl-peptides, perhaps as a result of misrecognition of the glycyl residue as an uncharged N-acyl group.
  • Inhibited by diisopropyl fluorophosphate.
  • Belongs to peptidase family S9C.
  • Formerly EC 3.4.14.3.
 2 A0A0B7H419 F9YQ51
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.
 1 A0A0B2QG91
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