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- , SAHase incubated with 100 μ DTNB alone was 70% inactivated in 30min. However, the inactivation by DTNB is slower in the presence of 62.5 μM substrate (6 times the Km); under the normal assay conditions, the rate of SAH cleavage at 30min is 75% of the initial rate. Part of this decrease may be due to substrate depletion (about 20% depletion of SAH in 30min in a typical assay)
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- , A possible explanation for the stoichiometry found in two experiments with I and one experiment with II is that recovery of fluoride is less efficient than the recovery of the unreacted inhibitor from the Centricon-30 filtration step used in these experiments. This is most likely due to nonspecific binding of fluoride anion to the protein under the conditions of low ionic strength, since in a control in the absence of protein, there was no difference between the recovery of fluoride and I.
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- , A mechanism for fluoride anion formation that does not involve nucleophilic attack is as follows: loss of the 2′ proton from the oxidized intermediate IV to give an enediol, tautomerization of the enediol to form a 2′-keto-3′,4′-didehydro-5′-deoxy-5′-fluoro intermediate, and finally elimination of fluoride with the generation of a4,5′-didehydro-2′,3′-diketone. However, this mechanism invokes an unnecessarily large number of steps. Also, there is no evidence to suggest that there is a base in the active site that is positioned for proton abstraction from the 2′ position: Palmer and Abeles12,13 have detected SAHase-catalyzed exchange at only the 4′ position in adenosine and 5′-deoxyadenosine.
- , The loss of the 3H-labeled adenine by a1,2 syn elimination or by a stepwise process would also be prevented by reduction of the carbonyl group at the 3′ position of an intermediate
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