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. 2011 Nov 23;287(3):1662–1669. doi: 10.1074/jbc.M111.281105

FIGURE 5.

FIGURE 5.

Human Cdc14A, human Cdc14B, and fission yeast Clp1 phosphatases exhibit selectivity for Ser(P). A, the rate of dephosphorylation of the indicated phosphopeptides by the hCdc14A(1–379) catalytic domain was compared at single substrate concentrations (250 μm for Ser(P) peptides and for Acm1pT31 and Cdc6pT7; 1 mm for all other Thr(P)-containing peptides). pS, Ser(P); pT, Thr(P). B, the rate of dephosphorylation of the indicated phosphopeptides by the hCdc14B(1–418) catalytic domain was compared at single substrate concentrations (500 μm for Acm1pS3 and Acm1pS31, 1 mm for all others). Data in A and B are averages of four trials with standard errors. C, dephosphorylation of Acm1pS31 (●) and Acm1pT31 (■) by fission yeast Clp1 was measured as a function of peptide concentration. Data were fit with the Michaelis-Menten equation containing a substrate inhibition term. Rates are expressed per pmol of Cdc14.