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- W32044903 abstract "Detailed kinetic studies of the inhibition of Alanine Racemase (5.1.1.1.) by the enantiomers of β chloroalanine reveal that the two enantiomers inhibit the enzyme at strikingly different levels and by different mechanisms. D chloroalanine inhibits at very low concentrations (Kj = .005 mM) in a competitive fashion. L chloroalanine inhibits only at much higher concentrations (Kj = 1.71 mM) and in a noncompetitive fashion. From these results it is postulated that the active site of the Alanine Racemase reacts asymmetrically with the enantiomers of the substrate and has a conformation which greatly favors the D enantiomer." @default.
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- W32044903 date "1976-02-01" @default.
- W32044903 modified "2023-09-23" @default.
- W32044903 title "Inhibition studies of the enantiomers of β chloroalanine on purified Alanine Racemase from B.subtilis" @default.
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- W32044903 doi "https://doi.org/10.1016/0006-291x(76)91215-8" @default.
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