CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.2010 | Zincin-like |
|
3.30.2010.30 |
Domain Context
CATH Clusters
| Superfamily | 3.30.2010.30 |
| 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 | |
| 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.
Chem.Biol.
|
