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Through kinetic studies, evidence is presented to show that the substrates of ATP-AMP phosphotransferase (EC 2.7.4.3), yeast adenylate kinase, are MgADP and ADP in the forward reaction. Various analogues of the substrates were studied to ascertain binding and catalytic limitations. Inhibitors such as 2'-AMP were shown to react at both catalytic sites. The kinetic studies and the Haldane relationship were consistent with the rapid equilibrium, random mechanism proposed for yeast adenylate kinase.
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Khoo et al. (1970) studied this question.
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