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. 2022 May 28;298(7):102089. doi: 10.1016/j.jbc.2022.102089

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© 2022 The Authors

This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

PMC Copyright notice

Development and testing of a novel glucan phosphatase inhibitor.A, the structure the TgLaforin inhibitor L319-21-M49. B, classification tree of the phosphatases used in this study. C, L319-M21-M49 inhibits TgLaforin activity against the model phosphatase substrate pNPP with >100-fold specificity over other phosphatases. D, Lineweaver-Burk double-reciprocal plot demonstrating that L319-21-M49 is a competitive inhibitor of TgLaforin. Each dataset represents a different inhibitor concentration, indicated in legend. E, L319-M21-M49 inhibits TgLaforin activity against soluble amylopectin; F, activity against insoluble starch with similar efficiency. All graphical error bars represent the standard deviation of at least three independent replicates, and all IC₅₀ values are the mean of three independent replicates with uncertainty presented as standard deviation from the mean. AP, alkaline phosphatase; CIP, calf intestinal phosphatase; DSP, dual-specificity phosphatase; PTP, protein tyrosine phosphatase; VHR, Vaccinia H1-related phosphatase.