Substrate specificity effects of lipoxygenase products and inhibitors on soybean lipoxygenase-1
| Autor: | Natalie K. Garcia, Aaron T. Wecksler, Theodore R. Holman |
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| Rok vydání: | 2009 |
| Předmět: |
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Molecular Linolenic acid Stereochemistry Linoleic acid Lipoxygenase Clinical Biochemistry Allosteric regulation Pharmaceutical Science Binding Competitive Biochemistry Article Substrate Specificity Linoleic Acid chemistry.chemical_compound Allosteric Regulation Drug Discovery Humans Lipoxygenase Inhibitors Molecular Biology chemistry.chemical_classification Arachidonic Acid biology Organic Chemistry Substrate (chemistry) Oleic acid Enzyme chemistry biology.protein Molecular Medicine Arachidonic acid Soybeans |
| Zdroj: | Bioorganic & Medicinal Chemistry. 17:6534-6539 |
| ISSN: | 0968-0896 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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