Abstract

The steady-state kinetics of the anaerobic reaction of soybean lipoxygenase-1 with linoleic acid and 13- l-hydroperoxylinoleic acid were studied. Initial rates of the formation of oxodienoic acids ∗∗ ∗∗ Oxodienoic acids: 1 : 1 mixture of 13-oxo-octadeca, 9,11-dienoic acid and 13-oxo-trideca, 9,11-dienoic acid. , absorbing at 285 nm, were measured at pH 10. About 50% of the consumed 13- l-hydroperoxylinoleic acid was converted into oxodienoic acids regardless of the initial ratio of the two substrates. A linear inhibition by both linoleic acid and 13- l-hydroperoxylinoleic acid was observed in the concentration range studied, which is on the upper side limited by the concentrations at which micelle- or acid-soap formation starts. A kinetic scheme is proposed based on one active site in lipoxygenase-1 which alternately binds the two substrates. Values for the kinetic constants were calculated by fitting simultaneously the complete set of data to the appropriate rate equation.

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