Leukotriene A4 Hydrolase (LTA4H)

Minami et al. (1987) reported the full-length cDNA and complete primary structure of human LTA4 hydrolase. This was the first report of the molecular cloning of an enzyme involved in the biosynthesis of eicosanoids. Funk et al. (1987) isolated a cDNA clone corresponding to leukotriene A4 hydrolase from a human lung lambda-gt11 expression library by immunoscreening with a polyclonal antiserum. Several additional clones from human lung and placenta cDNA lambda-gt11 libraries were obtained by plaque hybridization with the (32)P-labeled lung cDNA clone. One of the clones had an insert of 1,910 basepairs that contained a complete protein-coding region. From the deduced primary structure, leukotriene A4 hydrolase is a 610-amino acid protein with a calculated molecular weight of 69,140.