Graham A B, Park M V
Biochem J. 1969 Feb;111(3):257-62. doi: 10.1042/bj1110257.
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.
通过对牛肝线粒体辛酰辅酶A合成酶的产物抑制动力学进行研究,获得的证据与以下假设一致:该酶通过双底物-双产物乒乓机制起作用,底物和产物添加及释放的顺序为辅酶A、辛酸、辛酰辅酶A、ATP、焦磷酸(PP(i))和AMP。还有证据表明,不止一个辅酶A分子可以与该酶结合,并且它可能作为变构激活剂起作用。