Effect of citrate on the different reactions catalyzed by rat mammary gland acetyl CoA carboxylase.
The effect of citrate on the different reactions catalyzed by rat mammary gland acetyl CoA carboxylase has been investigated. Citrate showed modest effect on the ATP-orthophosphate and ATP-ADP exchange reactions. In contrast, this tricarboxylic acid caused marked concentration-dependent stimulation of the acetyl CoA-malonyl CoA exchange reaction which was concomitant with the activation of acetyl CoA carboxylation. The data obtained are consistent with the suggestion that activation by citrate of the overall forward reaction (malonyl CoA synthesis) primarily reflects enhancement of the carboxyltransferase half-reaction catalyzed by rat mammary gland acetyl CoA carboxylase.
D000103:Acetyl-CoA Carboxylase / Q000502:physiology*; D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001360:Avidin / Q000378:metabolism; D002384:Catalysis; D002951:Citrates / Q000494:pharmacology*; D005260:Female; D008025:Ligases / Q000502:physiology*; D008316:Malonyl Coenzyme A / Q000378:metabolism; D008321:Mammary Glands, Animal / Q000201:enzymology*; D010710:Phosphates / Q000378:metabolism; D051381:Rats
D002951:Citrates; D010710:Phosphates; D001360:Avidin; D008316:Malonyl Coenzyme A; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D008025:Ligases; D000103:Acetyl-CoA Carboxylase