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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 1: Leukotriene A(4) hydrolase

There are 4 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
Soluble epoxide hydrolase. [EC: 3.3.2.10]
An epoxide + H(2)O = a glycol.
  • Catalyzes the hydrolysis of trans-substituted epoxides, such as trans-stilbene oxide, as well as various aliphatic epoxides derived from fatty-acid metabolism.
  • It is involved in the metabolism of arachidonic epoxides (epoxyeicosatrienoic acids; EETs) and linoleic acid epoxides.
  • The enzyme from mammals is a bifunctional enzyme: the C-terminal domain exhibits epoxide-hydrolase activity and the N-terminal domain has the activity of EC 3.1.3.76.
  • Like EC 3.3.2.9, it is probable that the reaction involves the formation of an hydroxyalkyl-enzyme intermediate.
  • The enzyme can also use leukotriene A(4), the substrate of EC 3.3.2.6, but it forms 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than leukotriene B(4) as the product.
  • Formerly EC 3.3.2.3, EC 4.2.1.63 and EC 4.2.1.64.
 76 A0A0B0DHQ1 A0A0B0DHQ1 A0A0J7AYN0 A0A0J7AYN0 A0A1D8NLB9 A0A1D8NLB9 A0A1D9QAL0 A0A1D9QAL0 A0A3F3RBR7 A0A3F3RBR7
(66 more...)
Aminopeptidase B. [EC: 3.4.11.6]
Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.
  • Cytosolic or membrane-associated enzyme from mammalian tissues, activated by chloride ions and low concentrations of thiol compounds.
  • One of the activities of the bifunctional enzyme EC 3.3.2.6.
  • Belongs to peptidase family M1.
 3 O09175 Q8VCT3 Q9H4A4
Methionyl aminopeptidase. [EC: 3.4.11.18]
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
  • This membrane-bound enzyme, which is present in both prokaryotes and eukaryotes, releases the initiator methionine from nascent peptides.
  • The activity is dependent on the identity of the second, third and fourth amino acid residues of the target protein, but in general the enzyme acts only when the penultimate residue is small and uncharged (e.g. Gly, Ala, Cys, Ser, Thr, and Val).
  • Belongs to peptidase family M24A.
 2 G5E872 Q9HAU8
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.
 1 A6SAG8