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Fig. 4 | SpringerPlus

Fig. 4

From: Characterization of Lactobacillus salivarius alanine racemase: short-chain carboxylate-activation and the role of A131

Fig. 4

Kinetics of acetate inhibition of ALR and ALRA131K. a, b ALR and ALRA131K were assayed for 5 min at 30 °C and pH 7.0 (MES buffer) using various concentrations of l-alanine and acetate as the substrate and inhibitor, respectively. Shown are double reciprocal plots of the initial velocity of ALR (a) or ALRA131K (b) against l-alanine concentrations at several concentrations of acetate (n = 3 for each enzyme). Open circles, without acetate; filled circles, 1.0 mM acetate; open squares, 10.0 mM acetate; filled squares, 20.0 mM acetate; open triangles, 40.0 mM acetate

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