Abstract
The family of (S)-type lipoxygenases1 is characterized by a large sequence homology. A highly conserved histidine-rich motif2 includes the active center which contains a non-heme iron. The common characteristics of the reaction catalyzed by (S)-type lipoxygenases (LOX) include:3,4 i) substrates with a cis, cis-1,4-pentadiene structure, preferably in afree fatty acid, ii) a three step reaction mechanism consisting of hydrogen abstraction at C(3) of the pentadiene structure, oxygen attachment at C(1) or C(5) and reduction of the hydroperoxyl radial to the hydroperoxide, iii) formation of a conjugated cis, trans-diene structure, iv) redox cycling of the non-heme iron at the active center between Fe(III) and Fe(II) during the dioxygenation reaction, v) formation of an (S)-type chiral center at the oxidized carbon atom. On this basis, the large body of information originating, for example, from substrate specificity studies5 of (S)-type lipoxygenases can be summarized as a general (S)-type lipoxygenase reaction box model.6
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Lehmann, W.D. (1997). (S)-Type Lipoxygenase and Cyclooxygenase Reaction Box Models Characterizing the Stereochemistry of the Dioxygenation Reaction. In: Honn, K.V., Nigam, S., Marnett, L.J. (eds) Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation, and Radiation Injury 2. Advances in Experimental Medicine and Biology, vol 400. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5325-0_6
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DOI: https://doi.org/10.1007/978-1-4615-5325-0_6
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