Structural highlights
Function
LKHA4_YEAST Aminopeptidase that preferentially cleaves tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze an epoxide moiety of LTA(4) to form LTB(4) (in vitro).[1] [2] [3] [4] [5]
See Also
References
- ↑ Kull F, Ohlson E, Haeggstrom JZ. Cloning and characterization of a bifunctional leukotriene A(4) hydrolase from Saccharomyces cerevisiae. J Biol Chem. 1999 Dec 3;274(49):34683-90. PMID:10574934
- ↑ Kull F, Ohlson E, Lind B, Haeggstrom JZ. Saccharomyces cerevisiae leukotriene A4 hydrolase: formation of leukotriene B4 and identification of catalytic residues. Biochemistry. 2001 Oct 23;40(42):12695-703. PMID:11601994
- ↑ Tholander F, Kull F, Ohlson E, Shafqat J, Thunnissen MM, Haeggstrom JZ. Leukotriene A4 hydrolase, insights into the molecular evolution by homology modeling and mutational analysis of enzyme from Saccharomyces cerevisiae. J Biol Chem. 2005 Sep 30;280(39):33477-86. Epub 2005 Jul 15. PMID:16024909 doi:https://dx.doi.org/M506821200
- ↑ Thompson MW, Archer ED, Romer CE, Seipelt RL. A conserved tyrosine residue of Saccharomyces cerevisiae leukotriene A4 hydrolase stabilizes the transition state of the peptidase activity. Peptides. 2006 Jul;27(7):1701-9. Epub 2006 Apr 4. PMID:16597475 doi:https://dx.doi.org/10.1016/j.peptides.2006.02.006
- ↑ Helgstrand C, Hasan M, Uysal H, Haeggstrom JZ, Thunnissen MM. A Leukotriene A(4) Hydrolase-Related Aminopeptidase from Yeast Undergoes Induced Fit upon Inhibitor Binding. J Mol Biol. 2010 Dec 10. PMID:21146536 doi:10.1016/j.jmb.2010.11.059
