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. Author manuscript; available in PMC: 2014 Mar 26.
Published in final edited form as: Biochemistry. 2013 Mar 1;52(10):1725–1736. doi: 10.1021/bi3012077

Figure 1.

Figure 1

(a) Inhibition study of wt LRRK2 catalyzed phosphorylation of LRRKtide by Ponatinib. A: Plot of initial velocities vs [ATP] at [Ponatinib] = 1 (●), 0.3 (엯), 0.1 (▾), 0.04 (▿), 0.1 (∎), and 0 μM (□) all at a fixed LRRKtide concentration of 50 μM. B & C: Ponatinib concentration dependencies of (kcat)ATP and (kcat/Km)ATP apparent values derived from analysis of the data of panel A. (b) Inhibition study of the G2019S mutant catalyzed phosphorylation of LRRKtide by Ponatinib. A: Plot of initial velocities vs [ATP] at [Ponatinib] = 8 (●), 4 (엯), 2 (▾), 1 (▿), 0.5 (∎), and 0 μM (□) all at a fixed LRRKtide concentration of 50 μM. B & C: Ponatinib concentration dependencies of (kcat)ATP and (kcat/Km)ATP apparent values derived from analysis of the data of panel A.