Values of Km, Vmax, kcat and and the specificity constant (kcat/Km) for WT and C-Terminal Deletion Mutants of αGal.

Note. The values given are for the human enzyme purified from P. pastoris and assayed in triplicate followed by Lineweaver-Burk and non-linear regression analysis. Comparison of both Lineweaver-Burk and non-linear regression kinetic parameters show good general agreement (data not shown). Non-linear regression results are displayed above. The kcat was calculated using 90 kDa as the MW of αGal. A) MUG was used as the substrate for enzyme assay. Mean and standard deviation measurements are from multiple assays of three independent enzyme preparations for the Δ8 enzyme, two independent enzyme preparations for the WT enzyme, and single enzyme preparations for the other mutant enzymes. B) PNPαGal was used as the substrate for enzyme assay.Values of Km, Vmax, kcat and and the specificity constant (kcat/Km) for WT and C-Terminal Deletion Mutants of αGal.