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CATH Superfamily 3.40.220.10

Leucine Aminopeptidase, subunit E, domain 1

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:

"
Leucine Aminopeptidase, subunit E, domain 1
".

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 11: Leucine aminopeptidase 2, chloroplastic

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
Leucyl aminopeptidase. [EC: 3.4.11.1]
Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
  • Is activated by heavy metal ions.
  • Belongs to peptidase family M17.
  • Formerly EC 3.4.1.1.
 18 A0A0E0GE00 A0A0E0GE00 A0A0E0GE00 A0A178VYU7 A0A178VYU7 A2XAI5 A2XAI5 A2XAI5 P30184 P30184
(8 more...)
Prolyl aminopeptidase. [EC: 3.4.11.5]
Release of N-terminal proline from a peptide.
  • Present in the cytosol of mammalian and microbial cells.
  • In contrast to the mammalian form, the bacterial form of the enzyme hydrolyzes both polyproline and prolyl-2-naphthylamide.
  • The mammalian enzyme, which is not specific for prolyl bonds, is possibly identical with EC 3.4.11.1.
  • Belongs to peptidase family S33.
  • Formerly EC 3.4.1.4.
 18 A0A0E0GE00 A0A0E0GE00 A0A0E0GE00 A0A178VYU7 A0A178VYU7 A2XAI5 A2XAI5 A2XAI5 P30184 P30184
(8 more...)