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CATH Superfamily 1.25.40.320

Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal 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:

"
Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain
".

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 2: Leukotriene A(4) hydrolase

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
Leukotriene-A(4) hydrolase. [EC: 3.3.2.6]
(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H(2)O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate.
  • A bifunctional zinc metalloprotease that displays both epoxide hydrolase and aminopeptidase activities.
  • It preferentially cleaves tripeptides at an arginyl bond, with dipeptides and tetrapeptides being poorer substrates.
  • It also converts leukotriene A(4) into leukotriene B(4), unlike EC 3.2.2.10 which converts leukotriene A(4) into 5,6-dihydroxy- 7,9,11,14-eicosatetraenoic acid.
 14 A0A140VK27 A0A140VK27 A0A140VK27 H2Q6N3 H2Q6N3 H2Q6N3 P09960 P09960 P09960 P19602
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