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. 2010 Jul 2;38(20):7179–7186. doi: 10.1093/nar/gkq584

Figure 2.

Figure 2.

Loss of the aromatic interaction brings about the same reduction in kcat in the mycobacterial as in the human enzyme. (A and B) Michaelis–Menten curves of hDUT versus hDUTF158A (steady-state parameters in Table 1) and of mtDUT versus mtDUTH145A, respectively. (B) We evaluated the enzymatic activity of the mycobacterial dUTPase mutant in addition to the human one since our structural data was obtained using this readily crystallizable isoform. The rectangular hyperbolic fit to the Michaelis–Menten curves shown yielded kcat = 3.1 ± 0.06, KM = 0.46 ± 0.2 µM and kcat = 0.16 ± 0.001, KM = 0.56 ± 0.1 µM for mtDUT and mtDUTH145A, respectively.