mate and unlabeled MgATP yielded ~0.7 mol of the corresponding g-alcohol per mol glutamate. Their finding suggested that formation of the acyl-P as an internal enzyme-bound species is obviously highly favorable relative to solution-phase acyl-P formation.

The extraordinary power of positional isotope exchange experiments is now firmly established (Rose, 1982; Villafranca, 1989). As shown in Fig. 9.14, the positional isotope exchange procedure can be employed for any enzyme-catalyzed reaction in which the individual atoms of a functional group within a substrate, intermediate, or product, become torsionally equivalent during the course of a reaction. Positional isotope exchange experiments are employed with two goals: (a) to determine whether a particular intermediate is formed during catalysis; and (b) to evaluate the partition ratio of a particular enzyme-ligand complex (i.e., the fraction of the enzyme ligand complex that

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