Substrate specificity effects of lipoxygenase products and inhibitors on soybean lipoxygenase-1.
Recently, it has been shown that lipoxygenase (LO) products affect the substrate specificity of human 15-LO. In the current paper, we demonstrate that soybean LO-1 (sLO-1) is not affected by its own products, however, inhibitors which bind the allosteric site, oleyl sulfate (OS) and palmitoleyl sulfate (PS), not only lower catalytic activity, but also change the substrate specificity, by increasing the arachidonic acid (AA)/linoleic acid (LA) ratio to 4.8 and 4.0, respectively. The fact that LO inhibitors can lower activity and also change the LO product ratio is a new concept in lipoxygenase inhibition, where the goal is to not only reduce the catalytic activity but also alter substrate selectivity towards a physiologically beneficial product.
Wecksler
Aaron T
AT
Chemistry and Biochemistry Department, University of California, Santa Cruz, CA 95064, United States.
Garcia
Natalie K
NK
Holman
Theodore R
TR
D000494:Allosteric Regulation; D016718:Arachidonic Acid / Q000378:metabolism; D001667:Binding, Competitive; D006801:Humans; D019787:Linoleic Acid / Q000378:metabolism; D008084:Lipoxygenase / Q000737:chemistry / Q000378:metabolism*; D016859:Lipoxygenase Inhibitors / Q000494:pharmacology*; D008958:Models, Molecular; D013025:Glycine max / Q000201:enzymology*; D013379:Substrate Specificity
D016859:Lipoxygenase Inhibitors; D016718:Arachidonic Acid; D019787:Linoleic Acid; C101084:lipoxygenase L-1; D008084:Lipoxygenase