Molecular Cloning of a Novel Glucuronokinase/Putative Pyrophosphorylase from Zebrafish Acting in an UDP-Glucuronic Acid Salvage Pathway
Figure 7
Kinetics of DrGK for ATP and GlcA.
(A) Substrate saturation by Michaelis-Menten curve for ATP is shown. Activity of DrGK was measured with varying concentrations of ATP (0.01–1.4 mM) under standard conditions for 20 min with coupled HPLC enzyme assay. Km with 59.3 µM and Vmax 132.1 pkat/µg protein was calculated. Values are averages of three independently performed assays (+/− SD). (B) Substrate saturation by Michaelis-Menten curve for GlcA is shown. Activity of DrGK was measured with varying concentrations of GlcA (0.01–1.4 mM) under standard conditions for 20 min with coupled HPLC enzyme assay. Km with 31.3 µM and Vmax 137.6 pkat/µg protein was calculated. Values are averages of three independently performed assays (+/− SD).