| Abstract |
The aim of this study is to assess the inhibitory effects of L-phenylalanine on Placental Alkaline Phosphatase and understand the deviations in enzyme kinetics, as well as determine enzymatic parameters including Km, Vmax, and the inhibitor constant (Ki). The activity is assessed using simple enzyme kinetic assays with NPP as substrate, using UV-vis spectrophotometry measuring at 410nm, which is the optimal absorbance of NPP. The reading would generate Lineweaver-Burke plots that would be used to determine the deviations in enzymatic activity. The results displayed a decrease in enzymatic activity with increasing concentrations of L-phenylalanine inhibitor when compared to the standard enzyme assay with no inhibitor on Lineweakver-Burke plots. Therefore, L-phenylalanine is confirmed to be a competitive inhibitor for Placental Alkaline Phosphatases and decreases its enzymatic activity with increasing concentrations.
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