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- W1007107103 abstract "decarboxylases are known to catalyze their reaction in three steps [2, 8, 10, 11]. The proposed reaction suggests that a β-hydroxyacid (L-malate for the malic enzyme reaction and D-malate for the tartrate dehydrogenase reaction) is first oxidized to a β-ketoacid, which is decarboxylated to give an enol or enediol intermediate that is tautomerized to the final ketone product. A depiction of the tartrate dehydrogenase-catalyzed oxidative decarboxylation of D-malate is shown in Scheme 1. Multiple primary deuterium-primary 13C kinetic isotope effects have been instrumental in establishing the proposed mechanism [5–7, 15]. If one observes a finite primary deuterium isotope effect on the hydride transfer step and a finite primary 13C isotope effect on the decarboxylation step, data are consistent with both steps contributing to rate limitation of the overall reaction. The 13C effect is then repeated with the position for hydride transfer deuterated. A decrease in the observed 13C isotope effect with deuterated vs. protiumsubstituted substrate signals a stepwise oxidative decarboxylation reaction, while an increase or no change in the 13C isotope effect indicates a concerted reaction (no change would indicate the oxidative decarboxylation step is solely rate-determining)." @default.
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- W1007107103 title "Multiple isotope effects as a probe of the tartrate dehydrogenase-catalyzed oxidative decarboxylation of D-malate" @default.
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