The unusual action of (R,S)‐2‐hydroxy‐2‐trifluoromethyl‐trans‐n‐octadec‐4‐enoic acid on 5‐lipoxygenase from potato tubers

I. A. Butovich, V. A. Soloshonok, V. P. Kukhar

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


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 languageEnglish (US)
Pages (from-to)153-155
Number of pages3
JournalEuropean Journal of Biochemistry
Issue number1
StatePublished - Jul 1991

ASJC Scopus subject areas

  • Biochemistry


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