Figure 5 | Scientific Reports

Figure 5

From: Regulation of the Human Phosphatase PTPN4 by the inter-domain linker connecting the PDZ and the phosphatase domains

Figure 5

Phosphatase activity of PTPN4 bidomain constructs mutated in the linker. (a) Michaelis-Menten plots of initial rates of pNPP hydrolysis by different PTPN4 proteins at 600 nM without PDZ ligand; (b) Michaelis-Menten plots of initial rates of pNPP hydrolysis by different PTPN4 proteins at 600 nM in the presence of a saturated concentration of PDZ ligand (70–100 μM of Cyto8-RETEV);  linker-PTP;  PDZ-PTPWT;  F620G;  Q621G;  Y622G;  I623G. The solid lines are nonlinear least-squares fits of the data to the Michaelis-Menten equation. (c) kcat of PTPN4 constructs in the absence of PDZ ligand (light grey) and in the presence of PDZ ligand (Cyto8-RETEV) (dark grey). (d) KM of PTPN4 constructs in the absence of PDZ ligand (light grey) and in the presence of PDZ ligand (Cyto8-RETEV) (dark grey).

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