CATH Domain 3b7sA04

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	3B7S
External Links	PDBSum Proteopedia
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.