Substrate specificity effects of lipoxygenase products and inhibitors on soybean lipoxygenase-1

Bioorg Med Chem. 2009 Sep 15;17(18):6534-9. doi: 10.1016/j.bmc.2009.08.005. Epub 2009 Aug 8.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Allosteric Regulation
  • Arachidonic Acid / metabolism
  • Binding, Competitive
  • Humans
  • Linoleic Acid / metabolism
  • Lipoxygenase / chemistry
  • Lipoxygenase / metabolism*
  • Lipoxygenase Inhibitors / pharmacology*
  • Models, Molecular
  • Soybeans / enzymology*
  • Substrate Specificity

Substances

  • Lipoxygenase Inhibitors
  • Arachidonic Acid
  • Linoleic Acid
  • lipoxygenase L-1
  • Lipoxygenase