CATH Domain 3choA04

CATH Classification

Level	CATH Code	Description
	1	Mainly Alpha
	1.25	Alpha Horseshoe
	1.25.40	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
	1.25.40.320	Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain

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	3CHO
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Synthesis of glutamic acid analogs as potent inhibitors of leukotriene A4 hydrolase. Kirkland, T.A., Adler, M., Bauman, J.G., Chen, M., Haeggstrom, J.Z., King, B., Kochanny, M.J., Liang, A.M., Mendoza, L., Phillips, G.B., Thunnissen, M., Trinh, L., Whitlow, M., Ye, B., Ye, H., Parkinson, J., Guilford, W.J. Bioorg.Med.Chem.