Control of mitochondrial beta-oxidation flux.
The control of mitochondrial beta-oxidation, including the delivery of acyl moieties from the plasma membrane to the mitochondrion, is reviewed. Control of beta-oxidation flux appears to be largely at the level of entry of acyl groups to mitochondria, but is also dependent on substrate supply. CPTI has much of the control of hepatic beta-oxidation flux, and probably exerts high control in intact muscle because of the high concentration of malonyl-CoA in vivo. beta-Oxidation flux can also be controlled by the redox state of NAD/NADH and ETF/ETFH(2). Control by [acetyl-CoA]/[CoASH] may also be significant, but it is probably via export of acyl groups by carnitine acylcarnitine translocase and CPT II rather than via accumulation of 3-ketoacyl-CoA esters. The sharing of control between CPTI and other enzymes allows for flexible regulation of metabolism and the ability to rapidly adapt beta-oxidation flux to differing requirements in different tissues.
Eaton
Simon
S
Surgery Unit, Institute of Child Health, University College London, 30 Guilford Street, London WC1N 1EH, UK. s.eaton@ich.ucl.ac.uk
D000214:Acyl Coenzyme A / Q000378:metabolism*; D000818:Animals; D001692:Biological Transport; D002334:Carnitine O-Palmitoyltransferase / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D005227:Fatty Acids / Q000378:metabolism*; D005246:Feedback; D008928:Mitochondria / Q000201:enzymology*; D008929:Mitochondria, Heart / Q000378:metabolism; D008930:Mitochondria, Liver / Q000378:metabolism; D008931:Mitochondria, Muscle / Q000378:metabolism; D008954:Models, Biological; D010084:Oxidation-Reduction
D000214:Acyl Coenzyme A; D005227:Fatty Acids; D002334:Carnitine O-Palmitoyltransferase