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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 115207: N-acylaminoacyl-peptide hydrolase, isoform CRA_b

There are 1 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
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.
 10 A0A024R2U9 A0A0A7DUX9 B2GVB7 P13676 P13798 P19205 P80227 Q84LM4 Q8R146 V5QYZ9