Involvement of hysteretic effects in the inhibition of carnitine palmitoyltransferase by malonyl-CoA.
Carnitine palmitoyltransferase in its normal mitochondrial environment behaves as a hysteretic enzyme, exhibiting slow changes in reaction rate after the addition of oleoyl-CoA or malonyl-CoA. Reaction rates become constant after a short time, but the sensitivity of the enzyme from fed rats to the inhibition by malonyl-CoA remains much greater than that of starved rats.
D000214:Acyl Coenzyme A / Q000494:pharmacology*; D000217:Acyltransferases / Q000037:antagonists & inhibitors*; D000818:Animals; D002334:Carnitine O-Palmitoyltransferase / Q000037:antagonists & inhibitors*; D066298:In Vitro Techniques; D007700:Kinetics; D008297:Male; D008316:Malonyl Coenzyme A / Q000494:pharmacology*; D008930:Mitochondria, Liver / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains; D013217:Starvation / Q000201:enzymology
D000214:Acyl Coenzyme A; D008316:Malonyl Coenzyme A; D000217:Acyltransferases; D002334:Carnitine O-Palmitoyltransferase