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The alpha beta methylene analogs of adp and atp act as substrates for creatine kinase ec 2.7.3.2 change in gibbs free energy for this reaction and for the hydrolysis of the alpha beta methylene analog of atp


, : The alpha beta methylene analogs of adp and atp act as substrates for creatine kinase ec 2.7.3.2 change in gibbs free energy for this reaction and for the hydrolysis of the alpha beta methylene analog of atp. European Journal of Biochemistry 133(1): 169-172

The .alpha.beta.-methylene analogs of ATP and ADP, [.alpha.beta.CH2]ATP and [.alpha.beta.CH2]ADP, are substrates for [rabbit muscle] creatine kinase. However, the rate of the phosphoryl transfer reaction catalyzed is about 10-5 times lower than that with normal ATP. The affinities of the analogs (especially [.alpha.beta.CH2]ADP) for the enzyme are lower than those of the normal substrates. The equilibrium constant at 25.degree. C, measured using 31P NMR, for the reaction Mg[.alpha.beta.CH2]ATP + creatine .dblarw. Mg[.alpha.beta.Ch2]ADP + phosphocreatine + H+ is 2.2 .times. 10-12 M compared with a value of 2.5 .times. 10-10 M for the same reaction with the normal substrates, corresponding to a difference in .DELTA.G0 values of 11.7 kJ .cntdot. mol-1. It follows that .DELTA.G0 for the hydrolysis of the terminal phosphate group of Mg[.alpha.beta.CH2]ATP is less favorable by 11.7 kJ .cntdot. mol-1 than that for MgATP.

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