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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_3_0). At the point of the last release, this superfamily was named:

"
alpha/beta hydrolase
".

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 14: lysosomal Pro-X carboxypeptidase

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
Lysosomal Pro-Xaa carboxypeptidase. [EC: 3.4.16.2]
Cleavage of a -Pro-|-Xaa bond to release a C-terminal amino acid.
  • A lysosomal peptidase active at acidic pH that inactivates angiotensin II.
  • Inhibited by diisopropyl fluorophosphate.
  • Belongs to peptidase family S28.
  • Formerly EC 3.4.12.4.
 7 A0A024R5L0 A0A024R5L0 P42785 P42785 Q2TA14 Q5RBU7 Q7TMR0
Dipeptidyl-peptidase II. [EC: 3.4.14.2]
Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides.
  • A lysosomal serine-type peptidase maximally active at acidic pH.
  • Cleaves Lys-Ala-naphthylamide.
  • Belongs to peptidase family S28.
 3 Q9EPB1 Q9ET22 Q9UHL4