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. 2014 Feb 17;24(4):415–421. doi: 10.1016/j.cub.2013.12.052

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© 2014 The Authors

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Phosphorylation of PikI Activates Kinase Activity

(A) Quantification of PI(4,5)P₂ production over a range of substrate concentrations for wild-type and phosphomutants of PikI. Data represent mean ± SEM from four repeats using two different recombinant protein preparations.

(B) K_m (μM) and V_max (pmol PI(4,5)P₂/min/mg recombinant protein) of wild-type and phosphomutants of PikI, determined by fitting Michaelis-Menten curves to each data set and compared using a one-way ANOVA followed by Tukey’s post hoc test. ^∗p < 0.05.