Source:
recombinant C-terminal hexahistidine-tagged enzyme expressed in E. coli
·
Mr:
~69 kDa
·
Leukotriene A4 hydrolase (LTA4H) is a bifunctional zinc metalloenzyme that converts LTA4 into LTB4, a potent neutrophil chemoattractant.1 In addition to the hydrolase activity, LTA4H also exhibits anion-dependent aminopeptidase activity.1,2 LTA4H is a potential new drug target for a variety of indications associated with leukocyte infiltration to sites of inflammation. Cayman’s LTA4H (human recombinant) has been expressed and purified from E. coli. Both the epoxide hydrolase and aminopeptidase activities of the enzyme are functional as assessed by measurement of the separate enzyme activities. The enzyme therefore has application for the screening of inhibitors of LTB4 synthesis.
1
Haeggström, J.Z. Leukotriene A4 hydrolase/aminopeptidase, the gatekeeper of chemotactic leukotriene B4 biosynthesis. J Biol Chem 279(49) 50639-50642 (2004).
2
Rudberg, P.C., Tholander, F., Andberg, M., et al. Leukotriene A4 hydrolase: Identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates. J Biol Chem 279(26) 27376-27382 (2004).
Haeggström, J.Z. Leukotriene A4 hydrolase/aminopeptidase, the gatekeeper of chemotactic leukotriene B4 biosynthesis. J Biol Chem 279(49) 50639-50642 (2004).
Funk, C.D., Rådmark, O., Fu, J.Y., et al. Molecular cloning and amino acid sequence of leukotriene A4 hydrolase. Proc Natl Acad Sci USA 84 6677-6681 (1987).
Minami, M., Ohno, S., Kawasaki, H., et al. Molecular cloning of a cDNA coding for human leukotriene A4 hydrolase. Complete primary structure of an enzyme involved in eicosanoid synthesis. J Biol Chem 262 13873-13876 (1987).
Mancini, J.A., and Evans, J.F. Coupling of recombinant 5-lipoxygenase and leukotriene A4 hydrolase activities and transcellular metabolism of leukotriene A4 in Sf9 cells. Eur J Biochem 218 477-484 (1993).
Samuelsson, B., and Funk, C.D. Enzymes involved in the biosynthesis of leukotriene B4. J Biol Chem 264 19469-19472 (1989).
Rudberg, P.C., Tholander, F., Andberg, M., et al. Leukotriene A4 hydrolase: Identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates. J Biol Chem 279(26) 27376-27382 (2004).
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