Add time:08/23/2019         Source:sciencedirect.com

Publisher SummaryThis chapter describes the parallel inhibitions by 4-pentenoic acid of fatty acid oxidation and the two thiolases present in rat heart mitochondria. Experiments with purified 3-ketoacyl-CoA thiolase demonstrate that this enzyme is most rapidly inactivated by 3-keto-4-pentenoyl-CoA, a possible metabolite of 4-pentenoic acid. Rates of respiration supported by one of several substrates are then measured. Substrates used, their concentrations, and the rates of respiration observed in the absence of either n-pentanoate or 4-pentenoate are presented. Both acetoacetyl-CoA thiolase and 3-ketoacyl-CoA thiolase are inhibited to the same extent and at equal rates, which parallel initially the decrease in palmitoylcarnitine-supported respiration, n-pentanoate in contrast to 4-pentenoate is noninhibitory. Respiration supported by either octanoate or palmitoyl-CoA is inhibited by 4-pentenoate in a manner similar to that observed with palmitoylcarnitine as a substrate. The pyruvate-supported respiration is only slightly inhibited by both n-pentanoate and 4-pentenoate. It is suggested that the main cause for the inhibition of fatty acid oxidation by 4-pentenoate as reflected by the decreased respiratory rate is possibly the irreversible inactivation of 3-ketoacyl-CoA thiolase.

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