Inhibition of enzyme activities by free fatty acids.

نویسندگان

  • S V Pande
  • J F Mead
چکیده

The inhibition of several enzyme activities by free fatty acids has been examined. The inhibition of rat liver microsomal linolenate-activating enzyme activity by linolenate was found to be due to the inactivation of enzyme by substrate fatty acid. Stearoyl coenzyme A was also found to inhibit linolenate-activating enzyme. Likewise, microsomal glucose 6-phosphatase was inhibited by oleate; the extent of inhibition by oleate was related to the relative concentration of microsomal material. Citrate synthase from pig heart was inhibited by linoleate and glucose 6-phosphate dehydrogenase of yeast was inhibited by oleate. The inhibition of glucose 6-phosphate dehydrogenase was time-dependent and the presence of glucose 6-phosphate gave considerable protection against inactivation. The marked similarity in the observed inhibition of diverse enzymes by long chain unsaturated fatty acids to that of reported inhibitions by fatty acyl-CoA esters suggests that inhibitory effects are due to detergent properties of these inhibitors. In view of these and other considerations it is suggested that the extrapolation of observed inhibitions in vitro of enzyme activities by free fatty acids to regulation of metabolism in vivo must be made with caution.

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عنوان ژورنال:
  • The Journal of biological chemistry

دوره 243 23  شماره 

صفحات  -

تاریخ انتشار 1968