The N-terminal ß-barrel domain of mammalian lipoxygenases including mouse 5-lipoxygenase is not essential for catalytic activity and membrane binding…

Publication year: 2011 Source: Archives of Biochemistry and Biophysics, Available online 17 September 2011 Matthias Walther, Katharina Hofheinz, Robert Vogel, Jana Roffeis, Hartmut Kühn Mammalian lipoxygenases (LOXs) have been implicated in cell differentiation and in the pathogenesis of inflammatory and hyperproliferative diseases. The available structural information indicated that lipoxygenases constitute single polypeptide chain enzymes consisting of a small N-terminal ß-barrel domain and a larger C-terminal subunit that harbors the catalytic non-heme iron. Because of its structural similarity to C2-domains of lipases the N-terminal ß-barrel domain of lipoxygenases, which comprises about 110 amino acids, has been implicated in membrane binding and activity regulation

Publication year: 2011 Source: Archives of Biochemistry and Biophysics, Available online 17 September 2011 Matthias Walther, Katharina Hofheinz, Robert Vogel, Jana Roffeis, Hartmut Kühn Mammalian lipoxygenases (LOXs) have been implicated in cell differentiation and in the pathogenesis of inflammatory and hyperproliferative diseases. The available structural information indicated that lipoxygenases constitute single polypeptide chain enzymes consisting of a small N-terminal ß-barrel domain and a larger C-terminal subunit that harbors the catalytic non-heme iron. Because of its structural similarity to C2-domains of lipases the N-terminal ß-barrel domain of lipoxygenases, which comprises about 110 amino acids, has been implicated in membrane binding and activity regulation

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The N-terminal ß-barrel domain of mammalian lipoxygenases including mouse 5-lipoxygenase is not essential for catalytic activity and membrane binding…