CATH Classification

Domain Context

CATH Clusters

Superfamily Neutral Protease Domain 2
Functional Family Leukotriene A(4) hydrolase

Enzyme Information

3.3.2.6
Leukotriene-A(4) hydrolase.
based on mapping to UniProt P09960
(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.

UniProtKB Entries (1)

P09960
LKHA4_HUMAN
Homo sapiens
Leukotriene A-4 hydrolase

PDB Structure

PDB 4MS6
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Binding of Pro-Gly-Pro at the active site of leukotriene A4 hydrolase/aminopeptidase and development of an epoxide hydrolase selective inhibitor.
Stsiapanava, A., Olsson, U., Wan, M., Kleinschmidt, T., Rutishauser, D., Zubarev, R.A., Samuelsson, B., Rinaldo-Matthis, A., Haeggstrom, J.Z.
Proc.Natl.Acad.Sci.USA