Abstract
The 5-lipoxygenase from leukocytes catalyzes the oxidation of arachidonic acid to 5hydroperoxyeicosatetraenoic acid (5-HPETE) and leukotriene A4 (LTA4) as the first two steps of the leukotriene biosynthesis pathway. The reaction catalyzed by 5-lipoxygenase is similar to that of other mammalian and plant lipoxygenases, showing activation by the hydroperoxide product, kinetic lag phases and turnover-dependent inactivation, but with additional requirements for ATP, Ca2+1 and for a leukocyte protein (FLAP) presumably involved in the translocation of the enzyme to the membrane during cellular leukotriene production2.
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Riendeau, D., Denis, D., Falgueyret, JP., Percival, M.D., Gresser, M.J. (1991). Catalytic Properties and Reaction Mechanism of 5-Lipoxygenase. In: Bailey, J.M. (eds) Prostaglandins, Leukotrienes, Lipoxins, and PAF. GWUMC Department of Biochemistry Annual Spring Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0727-1_4
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