Sensitivity of carnitine acyltransferase I to malonly-CoA inhibition in isolated rat liver mitochondria is quantitatively related to hepatic malonyl-CoA concentration in vivo.
The sensitivity of carnitine acyltransferase I (EC 2.3.1.21) activity to malonyl-CoA inhibition in rat liver mitochondria isolated from animals in various physiological states was quantitatively proportional to the hepatic malonyl-CoA concentration in vivo. It is suggested that this relationship between the two parameters could result in a potent amplification mechanism for the reciprocal regulation of fatty acid synthesis and oxidation.
D000214:Acyl Coenzyme A / Q000494:pharmacology*; D000217:Acyltransferases / Q000037:antagonists & inhibitors*; D000818:Animals; D002334:Carnitine O-Palmitoyltransferase / Q000037:antagonists & inhibitors*; D005260:Female; D066298:In Vitro Techniques; D007774:Lactation; D008099:Liver / Q000032:analysis; D008316:Malonyl Coenzyme A / Q000032:analysis / Q000494:pharmacology*; D008930:Mitochondria, Liver / Q000187:drug effects / Q000201:enzymology*; D011247:Pregnancy; D051381:Rats
D000214:Acyl Coenzyme A; D008316:Malonyl Coenzyme A; D000217:Acyltransferases; D002334:Carnitine O-Palmitoyltransferase