This file contains calculations for the binding and enzyme kinetic parameter values, as well results for the multi-parametric sensitivity analyses and the parameter plausibility analyses.
The activities were measured as described in Materials and Methods. The KM and kcat for different substrates were derived by using varying concentrations (0.1 to 12 mM)) of individual substrates. The
KM and kcat/KM values for zebrafish wild-type and mutant enzyme are shown as means±S.D. (n = 3–6), and kcat values are derived from them. aNeither the zebrafish wild type nor the rat enzyme display si
