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- W2056512797 abstract "Abstract Homohypotaurine and homotaurine are transaminated by cell-free extracts of Pseudomonas fluorescens in the presence of α-ketoglutarate; the maximum rates of these transaminations are even higher than those observed for γ-aminobutyrate. The identity of the aminotransferase of homohypotaurine with aminobutyrate aminotransferase (EC 2.6.1.19) was demonstrated; equilibrium and kinetic constants were calculated for the different substrates. Homohypotaurine and homotaurine in the same extracts induce a reduction of NADP + or NAD + , in the presence of α-ketoglutarate. It is inferred from several results that the sulfinic and sulfonic aldehydes, resulting from the transamination step and characterized by thin-layer chromatography, are dehydrogenated in the presence of NADP + or NAD + , most probably by the succinate semialdehyde dehydrogenase (EC 1.2.1.16), to form the corresponding sulfinic and sulfonic acids; in this reaction, the rate of formation of the postulated 3-sulfopropionic acid is low as compared to that of succinic acid or to that of the postulated 3-sulfinopropionic acid. Neither taurine nor hypotaurine are substrates for the aminobutyrate aminotransferase of Ps. fluorescens ." @default.
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- W2056512797 date "1973-07-01" @default.
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- W2056512797 title "Sulfinic and sulfonic analogs of γ-aminobutyric acid and succinate semialdehyde, new substrates for the amino-butyrate aminotransferase and the succinate semialdehyde dehydrogenase of Pseudomonas fluorescens" @default.
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- W2056512797 doi "https://doi.org/10.1016/0005-2744(73)90128-9" @default.
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