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. Author manuscript; available in PMC: 2009 Dec 26.
Published in final edited form as: Chem Biol. 2009 Jun 26;16(6):605–612. doi: 10.1016/j.chembiol.2009.05.007

Figure 2.

Figure 2

(A) Efficient cleavage of the [G10] peptide by ClpP was observed in the presence of wild-type ClpX but not in the absence of ClpX or with ClpXE185Q, which cannot hydrolyze ATP. All reactions contained 10 µM of the [G10] substrate and 300 nM ClpP14. When present, the concentration of ClpX6 or the ATPase-defective mutant was 800 nM. (B) Degradation of different concentrations of the [VG]5 peptide by 800 nM ClpX6 and 300 nM ClpP14. (C) Steady-state rates of [VG]5 peptide degradation by ClpXP were calculated from the data in panel C and fit to the Michaelis-Menten equation (KM = 3.1 µM; Vmax = 12.7 min−1 ClpP−1).