Soybean lipoxygenase-1 kinetics are known to show product and substrat
e inhibition, With linoleic acid as the substrate and using a simple M
ichaelis-Menten formulation, we have shown that K-ss, the substrate in
hibition constant was increased by more than five-fold when initial ox
ygen concentration was increased from 228 to 1140 mu M. Excess substra
te inhibition is in fact almost avoided at high initial oxygen concent
ration, This modification seems correlated with enzyme saturation with
oxygen relative to linoleic acid, as reflected by alterations of the
substrate conversion rate, Possible implications for the enzyme kineti
cs are discussed. (C) 1997 Federation of European Biochemical Societie
s.