CATH Domain 5nidA04

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	5NID
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Capturing LTA4 hydrolase in action: Insights to the chemistry and dynamics of chemotactic LTB4 synthesis. Stsiapanava, A., Samuelsson, B., Haeggstrom, J.Z. Proc. Natl. Acad. Sci. U.S.A.