Leukotriene B4 hydroxydehydrogenase

From Proteopedia

Revision as of 08:08, 13 April 2016

spinqualitylabelsall models Guinea pig leukotriene B4 hydroxydehydrogenase complex with oxo-PGE2, NADP an Cl- ion (green)(PDB entry 1v3v) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Leukotriene B4 hydroxydehydrogenase/15-oxo-prostaglandin reductase (LB4H) is a bifunctional enzyme. It is part of the arachidonic acid cycle and is part of the metabolism of prostaglandins, leukotriene B4 and lipoxin. LB4H is san NADP-dependent enzyme. Relevance LB4H 1 restricts inflammation and confers resistance to tuberculosis infection[1]. Structural highlights LB4H active site is located at the hydrophobic pore on the dimer interface[2].

Structural highlights

3D Structures of Leukotriene B4 hydroxydehydrogenase

1zsv – LB4H - human
2dm6 –gpLB4H/15-oxo-prostaglandin 13-reductase+indomethacin – guinea pig
1v3t, 1v3u - gpLB4H/15-oxo-prostaglandin 13-reductase
1v3v - gpLB4H/15-oxo-prostaglandin 13-reductase+NADP+15-oxo-PGE-2

References

1. ↑ Tobin DM, Roca FJ, Ray JP, Ko DC, Ramakrishnan L. An enzyme that inactivates the inflammatory mediator leukotriene b4 restricts mycobacterial infection. PLoS One. 2013 Jul 11;8(7):e67828. doi: 10.1371/journal.pone.0067828. Print 2013. PMID:23874453 doi:http://dx.doi.org/10.1371/journal.pone.0067828
2. ↑ Hori T, Yokomizo T, Ago H, Sugahara M, Ueno G, Yamamoto M, Kumasaka T, Shimizu T, Miyano M. Structural basis of leukotriene B4 12-hydroxydehydrogenase/15-Oxo-prostaglandin 13-reductase catalytic mechanism and a possible Src homology 3 domain binding loop. J Biol Chem. 2004 May 21;279(21):22615-23. Epub 2004 Mar 8. PMID:15007077 doi:10.1074/jbc.M312655200