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Competitive inhibition of the 5-lipoxygenase-catalysed linoleate oxidation by arachidonic and 5-hydroperoxy-eicosatetraenoic acids.
Mirzoeva, O K; Sud'ina, G F; Pushkareva, M A; Varfolomeev, S D.
Affiliation
  • Mirzoeva OK; A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russian Federation.
FEBS Lett ; 377(3): 306-8, 1995 Dec 27.
Article in En | MEDLINE | ID: mdl-8549743
ABSTRACT
Linoleic and arachidonic acids are competing substrates for 5-lipoxygenase from barley. When these two substrates are added simultaneously, arachidonic acid acts as a competitive inhibitor of linoleic acid oxidation with Ki of 20 microM, the same value as the Michaelis constant for arachidonate oxygenation by this enzyme (22 +/- 3 microM). Linoleic acid hydroperoxide accumulated in the reaction mixture does not inhibit the enzymatic process, while arachidonic acid hydroperoxy product (5-hydroperoxy-6,8,11,14-eicosatetraenoic acid) inhibits it with very low Ki equal to 0.5 microM.
Subject(s)
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Collection: 01-internacional Database: MEDLINE Main subject: Linoleic Acids / Leukotrienes / Lipoxygenase Inhibitors / Arachidonic Acid Language: En Journal: FEBS Lett Year: 1995 Type: Article
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Linoleic Acids / Leukotrienes / Lipoxygenase Inhibitors / Arachidonic Acid Language: En Journal: FEBS Lett Year: 1995 Type: Article