Oxygen concentration determines regiospecificity in soybean lipoxygenase-1 reaction via a branched kinetic scheme.

The Journal of Biological Chemistry
H BerryV L Garde

Abstract

The effect of oxygen concentration on the regiospecificity of the soybean lipoxygenase-1 dioxygenation reaction was studied. At low oxygen concentrations (<5 microM), a dramatic change in the regiospecificity of the enzyme was observed with the hydroperoxy-octadecadienoic acid (HPOD) 13:9 ratio closer to 50:50 instead of the generally reported 95:5. This alteration of regiospecificity is not an isolated phenomenon, since it occurs during a reaction carried out under "classical" conditions, i.e. in a buffer saturated with air before the reaction. beta-carotene bleaching and electronic paramagnetic resonance findings provided evidence that substrate-derived free radical species are released from the enzyme. The kinetic scheme proposed by Schilstra et al. (Schilstra, M. J., Veldink, G. A. & Vliegenthart, J. F. G. (1994) Biochemistry 33, 3974-3979) was thus expanded to account for the observed variations in specificity. The equations describing the branched scheme show two different kinetic pathways: a fully enzymatic one leading to a regio-isomeric composition of 13-HPOD:9-HPOD = 95:5, and a semienzymatic one leading to a regio-isomeric composition of 13-HPOD:9-HPOD = 50:50. The ratio between the two different pathways depends on ...Continue Reading

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Apr 21, 1999·Progress in Lipid Research·A Grechkin
Sep 22, 2001·Biochimica Et Biophysica Acta·F ClemensP Frohberg
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Aug 31, 2014·Food Chemistry·Stéphanie BrandicourtAnne-Marie Riquet
Jan 1, 2017·Comprehensive Reviews in Food Science and Food Safety·Stefan HaywardPieter Swart

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