CATH Classification

Domain Context

CATH Clusters

Superfamily Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain
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 3FH8
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Discovery of 4-[(2S)-2-{[4-(4-chlorophenoxy)phenoxy]methyl}-1-pyrrolidinyl]butanoic acid (DG-051) as a novel leukotriene A4 hydrolase inhibitor of leukotriene B4 biosynthesis.
Sandanayaka, V., Mamat, B., Mishra, R.K., Winger, J., Krohn, M., Zhou, L.M., Keyvan, M., Enache, L., Sullins, D., Onua, E., Zhang, J., Halldorsdottir, G., Sigthorsdottir, H., Thorlaksdottir, A., Sigthorsson, G., Thorsteinnsdottir, M., Davies, D.R., Stewart, L.J., Zembower, D.E., Andresson, T., Kiselyov, A.S., Singh, J., Gurney, M.E.
J.Med.Chem.
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