Crystallization and resolution of the lipoxygenase of Pseudomonas aeruginosa 42A2 and phylogenetic study of the subfamilies of the lipoxygenases

Abstract

Lipoxygenases are non-heme iron enzymes essential in eukaryotes, where they catalyze the formation of the fatty acid hydroperoxides that are required by a large diversity of biological and pathological processes. In prokaryotes, most of them totally lacking in polyunsaturated fatty acids, the possible biological roles of lipoxygenases have remained obscure. In this study, it is reported the crystallization of a lipoxygenase of Pseudomonas aeruginosa (Pa_LOX), the first from a prokaryote. High resolution data has been acquired which is expected to yield structural clues to the questions adressed. Besides, a preliminar phylogenetic analysis using 14 sequences has confirmed the existence of this subfamily of bacterial lipoxygenases, on one side, and a greater diversity than in the corresponding eukaryotic ones, on the other. Finally, an evolutionary study of bacterial lipoxygenases on the same set of lipoxygenases, show a selection pressure of a basically purifying or neutral character except for a single aminoacid, which would have been selected after a positive selection event.