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• W2073443144 abstract "Abstract 1. In the presence of the hypoglycin metabolites methylenecyclopropylpyruvate (MCPP) and methylenecyclopropylacetate (MCPA), rat liver mitochondria oxidized palmitoyl-carnitine only as far as butyrate and at a decreased rate. Although pent-4-enoic acid (pent-4-enoate) inhibited the rate of β-oxidation of palmitoyl-carnitine by mitochondria, the oxygen uptake was consistent with the complete oxidation of the substrate. 2. The inhibition of β-oxidation by pent-4-enoate was partially reversed by very high concentrations of l -carnitine. Conditions were also defined for the sustained oxidation of pent-4-enoate by mitochondria. 3. Pent-4-enoate inhibited pyruvate oxidation, but only at concentrations much higher than those needed to inhibit β-oxidation. MCPA had no effect on either pyruvate or 2-oxoglutarate oxidation in mitochondria. 4. Soluble extracts of rat or ox liver mitochondria completely oxidized pent-4-enoyl-CoA and the oxidation of butyryl-CoA added subsequently was unaffected. Incubation of soluble extracts with pent-4-enoyl-CoA in the absence of cofactors caused inhibition of acetoacetyl-CoA thiolase activity. However, this enzyme was not inhibited in intact mitochondria by pent-4-enoate. 5. MCPA specifically inhibited butyryl-CoA dehydrogenase in both intact mitochondria and in soluble extracts supplemented with ATP and CoASH. 6. Both MCPP and MCPA (1 mM) caused a rapid decrease in CoASH concentrations in mitochondria; acetyl-CoA concentrations were unaffected. Concentrations of pent-4-enoate (20 μM) sufficient to inhibit β-oxidation caused only a slight decrease in CoASH whereas higher concentrations (0.1–1.0 mM) caused a more extensive depletion of CoASH. However, evidence is presented to suggest that CoASH depletion is not the mechanism by which these compounds inhibit β-oxidation. 7. Pent-4-enoate and MCPA were substrates for butyryl-CoA synthetase. Km and Vmax values for several unusual, straight and branched chain fatty acids were determined. 8. Some short-chain acyl-CoA esters were substrates for an acyl-CoA hydrolase located in the mitochondrial matrix. 9. Some short-chain acyl-CoA esters competitively inhibited the activation of pyruvate carboxylase by acetyl-CoA. 10. The possible mechanisms by which hypoglycin and pent-4-enoate cause inhibition of β-oxidation and hypoglycaemia in vivo are discussed." @default.
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• W2073443144 date "1978-01-01" @default.
• W2073443144 modified "2023-10-18" @default.
• W2073443144 title "Mechanisms of the metabolic disturbances caused by hypoglycin and by pent-4-enoic acid. In vitro studies." @default.
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• W2073443144 doi "https://doi.org/10.1016/0006-2952(78)90204-6" @default.
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