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Fig. 3 | BMC Biochemistry

Fig. 3

From: Identification of inhibitors that target dual-specificity phosphatase 5 provide new insights into the binding requirements for the two phosphate pockets

Fig. 3

Michaelis-Menten Kinetics. a Michaelis-Menten plot of DUSP5 PD(WT) initial velocity versus substrate (pNPP) concentration, monitoring production of p-nitrophenolate at 405 nm. Reaction was in 100 mM Tris-HCl (pH 7.5), 100 mM NaCl, 5 mM MgCl2 and 1 mM DTT, and was initiated with enzyme. The line represents a nonlinear least squares fit to equation 1. b Enzymatic rate as a function of DMSO concentration (% v/v), and at a fixed level of pNPP (5 mM), with other conditions as in panel (a). Relative enzyme activation represents the rate normalized to that obtained at 0 % DMSO

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BMC Biochemistry

ISSN: 1471-2091

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