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CATH Superfamily 3.40.50.880

Class I glutamine amidotransferase (GATase) 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 8827: Peptidase E

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
Dipeptidase E. [EC: 3.4.13.21]
Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides.
  • A free carboxy group is not absolutely required in the substrate since Asp-Phe-NH(2) and Asp-Phe-OMe are hydrolyzed somewhat more slowly than dipeptides with free C-termini.
  • No peptide larger than a C-blocked dipeptide is known to be a substrate.
  • Asp-NH-Np is hydrolyzed and is a convenient substrate for routine assay.
  • The enzyme is most active near pH 7.0, and is not inhibited by di-isopropylfluorophosphate or phenylmethanesulfonyl fluoride.
  • Belongs to peptidase family S51.
 1 P58493