We found that (R,S)‐2‐hydroxy‐2‐trifluoromethyl‐trans‐n‐octadec‐4‐enoic acid (HTFOA) is a powerful activator of 5‐lipoxygenase from potato tubers. The degree of activation of the enzyme is proportional to the HTFOA concentration and is a maximum at about 0.1 mM independently of initial substrate concentration (25 μM or 0.1 mM). At greater concentrations of HTFOA, enzyme inhibition takes place. Enzyme activation is inversely proportional to the substrate (linoleic acid) concentration. The results may be explained by assuming that a regulatory center exists in the enzyme molecule, which shows affinity to both substances: activator and linoleic acid.
|Original language||English (US)|
|Number of pages||3|
|Journal||European Journal of Biochemistry|
|State||Published - Jul 1991|
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