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- W2098544099 abstract "Fatty acid synthesis via the citrate cleavage pathway requires the continual replenishment of oxaloacetate within the mitochondria, probably by carboxylation of pyru- vate. Malic enzyme, although present in adipose tissue, is com- pletely localized in the cytoplasm and has insufficient activity to support lipogenesis. Pyruvate carboxylase was found to be active in both the mitochondria and cytoplasm of epididymal adipose tissue cells; it was dependent on both ATP and biotin. Alterations in dietary conditions induced no significant changes in mitochondrial pyruvate carboxylase activity, but the soluble activity was depressed in fat-fed animals. The possible importance of the soluble activity in lipogenesis lies in its participation in a soluble malate transhydrogenation cycle with NAD malate dehydrogenase and malic enzyme, whereby a continual supply of NADPH is produced. Conse- quently, the pyruvate carboxylase in adipose tissue both gen- erates mitochondrial oxaloacetate for the citrate cleavage pathway and supplies soluble NADPH for the conversion of acetyl-coA to fatty acid." @default.
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- W2098544099 date "1967-03-01" @default.
- W2098544099 modified "2023-10-12" @default.
- W2098544099 title "The citrate cleavage pathway and lipogenesis in rat adipose tissue: replenishment of oxaloacetate" @default.
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- W2098544099 doi "https://doi.org/10.1016/s0022-2275(20)38917-3" @default.
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