| Literature DB >> 4304157 |
Abstract
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.Entities:
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Year: 1969 PMID: 4304157 PMCID: PMC1187506 DOI: 10.1042/bj1110257
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857