Is ATP a substrate for 15-lipoxygenase?
作者： Rajkumar Kumarathasan , Frans HH Leenen
DOI: 10.1139/O99-073
关键词:
摘要: Lipoxygenases catalyze peroxidation of polyunsaturated fatty acids containing the 1-cis, 4-cis pentadiene structure. Linoleic (18:2), linolenic (18:3), and arachidonic (20:4) are predominant substrates for this class enzymes. Effects 15-lipoxygenase on hydrolysis adenosine 5'-triphosphate were investigated in vitro using soybean lipoxygenase 5'-[gamma-32P]triphosphate. The amount inorganic phosphate released from was dependent upon enzyme as well substrate concentrations, pH, duration incubation. ATPase activity with a Vmax value 3.3 mumol.mg protein-1.h-1 Km 5.9 mM noted presence different concentrations ATP at pH = 7.4. Phenidone, inhibitor, had no effect reaction. These findings suggest that catalyzes release primarily via hydrolysis.
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