. Author manuscript; available in PMC: 2008 Oct 23.

Published in final edited form as: Biochemistry. 2007 Sep 29;46(42):11780–11788. doi: 10.1021/bi701408t

Table 3.

Comparison of TNP-ATP Binding to Wild-Type and Mutant PMKs ^a

Enzyme	S_½^b (μM)	n^c
WT	2.3±0.2	0.9
R110M	3.1±0.1	1.2
R141M	3.9±0.2	1.2

Fluorescent titrations were performed in 100 mM MOPS, 100 mM KCl, 1 mM DTT (pH 7.0) at 25°C.

S_½ ([ligand] at half maximal binding) values were estimated by fitting the titration data to the nonlinear regression equation y = B_max[X]/(S_½ + [X]). Errors represent the standard error of the fit.

The n value (binding stoichiometry) was estimated by Scatchard analysis.