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. 2013 Jun 16;288(31):22493–22505. doi: 10.1074/jbc.M113.468595

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© 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 3. — pH-dependent inactivation of (BACCR)NAT3 by IAA. The first-order inactivation constant (k_inact) was determined between pH 6 and 9.5 by measuring the ln of residual activity after 1 mm IAA inactivation of the enzyme. The non-linear fit of data to the Henderson-Hasselbalch equation (Equation 2) indicates pK_a values of 8.26 and 7.80 for the Cys⁶⁹ catalytic residue of the wild type (black curve) and E123D mutant (red curve), respectively. Standard error bars are shown for three independent experiments.