Carnitine palmitoyltransferase. Activation by palmitoyl-CoA and inactivation by malonyl-CoA

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Abstract

Extraction of rat liver mitochondria twice with 0.5% Triton X-100 in a salt-free medium leaves less than 10% of the carnitine palmitoyltransferase membrane bound. The remaining membrane-bound enzyme is inhibited virtually completely by 10 μM malonyl-CoA. Preincubation of the extracted membranes with palmitoyl-CoA and salts (KC1) for several minutes activates the enzyme and makes it increasingly insensitive to malonyl-CoA. Addition of malonyl-CoA to the preincubation reverses this desensitization. In albumin-containing media salts also decrease the binding of palmitoyl-CoA to albumin and stimulate carnitine palmitoyltransferase by increasing substrate availability in free solution. The reverse reaction shows accelerated desensitization by palmitoylcarnitine and resensitization by malonyl-CoA. © 1985.

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Bremer, J., Woldegiorgis, G., Schalinske, K., & Shrago, E. (1985). Carnitine palmitoyltransferase. Activation by palmitoyl-CoA and inactivation by malonyl-CoA. Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism, 833(1), 9–16. https://doi.org/10.1016/0005-2760(85)90247-4

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