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Inhibition of prostaglandin endoperoxide synthetase by thiol analogues of prostaglandin.

Authors
  • S Ohki
  • N Ogino
  • S Yamamoto
  • O Hayaishi
  • H Yamamoto
Publication Date
Jan 01, 1977
Source
PMC
Keywords
License
Unknown

Abstract

A variety of thiol compounds inhibited the enzymatic bis-oxygenation of 8,11,14-eicosatrienoic acid to prostaglandin G1, as examined with a purified preparation of prostaglandin endoperoxide synthetase (prostaglandin synthase; 8,11,14-eicosatrienoate, hydrogen-donor:oxygen oxidoreductase; EC 1.14.99.1) from bovine vesicular gland. The hydroperoxide cleavage of prostaglandin G1 producing prostaglandin H1 was not affected by these thiol compounds. Several prostaglandin analogues with a thiol group (9,11-dihydroxy-15S- or 15R-mercaptoprosta-5,13-dienoic acid, 1-mercapto-9,11,15-trihydroxyprosta-5,13-diene, and 1-mercapto-9-oxo-11,15-dihydroxyprosta-5,13-diene) were most potent inhibitors, showing almost complete inhibition at concentrations on the order of 1 muM. Other thiol compounds, such as 2,3-dimercaptopropanol, dithiotherreitol, and dihydrolipoic acid, were also inhibitory but were much less effective. The inhibition, as examined with 9,11-dihydroxy-15S-mercaptoprosta-5,13-dienoic acid and 2,3-dimercaptopropanol, was noncompetitive.

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