A product-inhibition study of the mechanism of mitochondrial octanoly-coenzyme A synthetase.
By a study of the product-inhibition kinetics of the octanoyl-CoA synthetase from ox liver mitochondria, evidence was obtained consistent with the hypothesis that the enzyme reacts by a Bi Uni Uni Bi Ping Pong type of mechanism in which the order of addition and evolution of substrates and products is CoA, octanoate, octanoyl-CoA, ATP, PP(i) and AMP. There is also evidence that more than one molecule of CoA can add to the enzyme and that it may act as an allosteric activator.
D000227:Adenine Nucleotides / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002210:Caprylates / Q000378:metabolism*; D002417:Cattle; D003065:Coenzyme A / Q000378:metabolism*; D003864:Depression, Chemical; D011756:Diphosphates / Q000378:metabolism; D066298:In Vitro Techniques; D007700:Kinetics; D008025:Ligases / Q000378:metabolism*; D008930:Mitochondria, Liver / Q000201:enzymology*; D008956:Models, Chemical
D000227:Adenine Nucleotides; D002210:Caprylates; D011756:Diphosphates; D000255:Adenosine Triphosphate; D008025:Ligases; D003065:Coenzyme A