Use of mitochondrial inner membrane proteins and phospholipids to facilitate disengagement of the catalytic and malonyl-CoA binding components of carnitine palmitoyltransferase from liver mitochondrial outer membranes.
1. It was shown by Ghadiminejad and Saggerson (1991) that the anionic detergent cholate caused disengagement of the malonyl-CoA binding entity from the catalytic entity of outer membrane carnitine palmitoyltransferase (CPT1). 2. This disengagement was only observed if inner membrane material was present. 3. It is now shown that this effect is mimicked by a CPT-free inner membrane protein fraction together with an inner membrane lipid extract or with individual phospholipids (phosphatidylcholine, phosphatidylethanolamine or diphosphatidylglycerol). 4. The lipids alone have no effect but act synergistically with the inner membrane protein fraction.
Ghadiminejad
I
I
Department of Biochemistry and Molecular Biology, University College London, U.K.
Saggerson
D
D
D000818:Animals; D002334:Carnitine O-Palmitoyltransferase / Q000378:metabolism*; D002384:Catalysis; D007425:Intracellular Membranes / Q000378:metabolism; D008297:Male; D008316:Malonyl Coenzyme A / Q000378:metabolism; D008563:Membrane Lipids / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D008930:Mitochondria, Liver / Q000201:enzymology / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D008563:Membrane Lipids; D008565:Membrane Proteins; D010743:Phospholipids; D008316:Malonyl Coenzyme A; D002334:Carnitine O-Palmitoyltransferase