Leukotriene A4 Hydrolase

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spinqualitylabelsall models Human leukotriene A4 Hydrolase complex with bestatin, acetate, imidazole, Yb+3 (green) and Zn+2 (grey) ions (PDB entry 1hs6) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Disease 4 Structural highlights Function Leukotriene A4 Hydrolase (LTA4H) is an aminopeptidase which converts leukotriene A4 to leukotriene B4 as part of the arachidonic acid metabolism[1] . LTA4H is a bifunctional Zn+2 enzyme. Relevance LTA4H inhibitors have potential in targeting chronic, autoimmune-driven inflammation[2] . Disease Mutations in LTA4H are linked to susceptibility to asthma and to cardiovascular disease. Structural highlights LTA4H structure shows 3 domains: N-terminal, catalytic and C-terminal. The catalytic domain is made of 2 lobes: an α-helical one and an α/β one. The catalytic site is located between the 2 lobes and contains a Zn+2 ion[3] .

3D Structures of Leukotriene A4 Hydrolase

Updated on 17-April-2016

References

1. ↑ Paige M, Wang K, Burdick M, Park S, Cha J, Jeffery E, Sherman N, Shim YM. Role of leukotriene A4 hydrolase aminopeptidase in the pathogenesis of emphysema. J Immunol. 2014 Jun 1;192(11):5059-68. doi: 10.4049/jimmunol.1400452. Epub 2014, Apr 25. PMID:24771855 doi:http://dx.doi.org/10.4049/jimmunol.1400452
2. ↑ Fourie AM. Modulation of inflammatory disease by inhibitors of leukotriene A4 hydrolase. Curr Opin Investig Drugs. 2009 Nov;10(11):1173-82. PMID:19876785
3. ↑ Thunnissen MM, Nordlund P, Haeggstrom JZ. Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation. Nat Struct Biol. 2001 Feb;8(2):131-5. PMID:11175901 doi:10.1038/84117