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.
Ghadiminejad
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I
Department of Biochemistry, University College London, UK.
Saggerson
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ED
D000214:Acyl Coenzyme A / Q000494:pharmacology*; D000217:Acyltransferases / Q000037:antagonists & inhibitors*; D000818:Animals; D002334:Carnitine O-Palmitoyltransferase / Q000037:antagonists & inhibitors*; D002352:Carrier Proteins / Q000378:metabolism*; D007425:Intracellular Membranes / Q000201:enzymology*; D007700:Kinetics; D008316:Malonyl Coenzyme A / Q000378:metabolism / Q000494:pharmacology*; D008930:Mitochondria, Liver / Q000201:enzymology*; D051381:Rats; D013367:Submitochondrial Particles / Q000201:enzymology*
D000214:Acyl Coenzyme A; D002352:Carrier Proteins; D008316:Malonyl Coenzyme A; D000217:Acyltransferases; D002334:Carnitine O-Palmitoyltransferase