CATH Classification

Domain Context

CATH Clusters

Superfamily 1.10.1740.60
Functional Family

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 3B7T
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure-based dissection of the active site chemistry of leukotriene a4 hydrolase: implications for m1 aminopeptidases and inhibitor design.
Tholander, F., Muroya, A., Roques, B.P., Fournie-Zaluski, M.C., Thunnissen, M.M., Haeggstrom, J.Z.
Chem.Biol.