A product-inhibition study of the mechanism of mitochondrial octanoly-coenzyme A synthetase.
نویسندگان
چکیده
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.
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ورودعنوان ژورنال:
- The Biochemical journal
دوره 111 3 شماره
صفحات -
تاریخ انتشار 1969