Figure 8
(A) Michaelis–Menten plot of the l-Ser β-elimination catalyzed by mouse SR. Km and kcat values for the l-Ser dehydration were determined to be 3.5 ± 0.4 mM and 97 ± 4 min−1, respectively. Data were represented as means ± SD (error bars) of three independent experiments. (B) The Lineweaver–Burk plot of the l-Ser β-elimination reaction on inhibitor l-β-EHAsn concentration (0, 50, 100, 200 µM). The l-Ser β-elimination activity was inhibited by l-β-EHAsn with the Ki value of 40 ± 6 µM, which was estimated by global fitting to a mixed model inhibition equation using GraphPad Prism software α value of 19, R2 = 0.98). Note that the data was also well fitted to a competitive inhibition equation (R2 = 0.98). Reactions were carried out as described in Materials and Methods. Each data point represents mean of two independent experiments.
Inhibition of mouse serine racemase by l-β-EHAsn

(A) Michaelis–Menten plot of the l-Ser β-elimination catalyzed by mouse SR. Km and kcat values for the l-Ser dehydration were determined to be 3.5 ± 0.4 mM and 97 ± 4 min−1, respectively. Data were represented as means ± SD (error bars) of three independent experiments. (B) The Lineweaver–Burk plot of the l-Ser β-elimination reaction on inhibitor l-β-EHAsn concentration (0, 50, 100, 200 µM). The l-Ser β-elimination activity was inhibited by l-β-EHAsn with the Ki value of 40 ± 6 µM, which was estimated by global fitting to a mixed model inhibition equation using GraphPad Prism software α value of 19, R2 = 0.98). Note that the data was also well fitted to a competitive inhibition equation (R2 = 0.98). Reactions were carried out as described in Materials and Methods. Each data point represents mean of two independent experiments.

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