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- W339799824 abstract "The NAD-malic enzyme from Ascaris suum catalyzes the divalent metal ion dependent oxidative decarboxylation of L-malate to yield pyruvate, carbon dioxide and NADH. Multiple isotope effect studies suggest a stepwise chemical mechanism with hydride transfer from L-malate to NAD occurring first to form oxalacetate, followed by decarboxylation. Utilizing L-malate-2-T, tritium V/K isotope effects have been determined for the hydride transfer step using a variety of alternative dinucleotide substrates and divalent metal ions. Combination of these data with deuterium isotope effects data and previously determined [sup 13]C isotope effects has allowed the calculation of intrinsic isotope effects for the malic enzyme catalyzed reaction. The identity of both the dinucleotide substrate and divalent metal ion has an effect of the size of the intrinsic isotope effect for hydride transfer." @default.
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- W339799824 date "1992-01-01" @default.
- W339799824 modified "2023-09-23" @default.
- W339799824 title "Malic enzyme: Tritium isotope effects with alternative dinucleotide substrates and divalent metal ions" @default.
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