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- W2170423302 abstract "1 A preparation of malic enzyme was made from chicken liver. 2 The enzyme was incubated, in tritiated buffer containing NADP, with 2S, 3S-[2,3-2H2]malate. A third malate, 2S, 3R-[3-3H1]malate, was incubated with the enzyme, NADP, and unlabelled buffer. Conditions were chosen so that the initially formed pyruvate was converted into lactate, which was isolated. 3 The lactate from each of the three incubations was oxidized chemically to acetate, which was purified. 4 Each specimen of acetate was assayed for chirality by the previously established method of conversion into S-malate by condensation with glyoxylate on malate synthase, and measuring the fractional loss of tritium on incubation of the S-malate with fumarate hydratase. 5 In this way, the acetate derived from 2S, 3R-[3-2H1]malate was shown to have S chirality and the acetate derived from 2S, 3S-[2,3-2H2]malate was shown to have R chirality. As expected, the acetate from 2S, 3R-[3-3H1]malate was found non-chiral. 6 It is deduced that when S malate is decarboxylated on malic enzyme, carboxyl is replaced by hydrogen without net change of configuration. This confirms a result obtained by Rose in 1970 by different methods." @default.
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- W2170423302 date "1972-04-01" @default.
- W2170423302 modified "2023-09-25" @default.
- W2170423302 title "Stereochemical Course of Decarboxylation of S-Malate on Malic Enzyme" @default.
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- W2170423302 doi "https://doi.org/10.1111/j.1432-1033.1972.tb01780.x" @default.
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