Carnitine palmitoyltransferase (CPT2) from liver mitochondrial inner membrane becomes inhibitable by malonyl-CoA if reconstituted with outer membrane malonyl-CoA binding protein.

A soluble extract was obtained on treatment of rat liver mitochondrial outer membranes with cholate which bound [14C]malonyl-CoA but was essentially free of carnitine palmitoyltransferase (CPT) activity. Extraction of mitochondrial inner membranes with cholate readily solubilized a CPT activity which was insensitive to malonyl-CoA. Combination of these two extracts caused the CPT derived from inner membranes to become inhibitable by malonyl-CoA.