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Figure 3

From: Enzyme mechanistic studies of NMA1982, a protein tyrosine phosphatase and potential virulence factor in Neisseria meningitidis

Figure 3

Assessing NMA1982 phosphatase activity. (a) Principle of the DiFMUP NMA1982 fluorescence intensity assay. (b) Michaelis–Menten kinetics for NMA1982 using DiFMUP as the substrate. (c) Hydrogen bonding interactions between the side chain of R136 and the backbone oxygen atoms of WPD-loop residues A69, R70, and I72 in NMA1982 restrict WPD-loop dynamics.

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