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. Author manuscript; available in PMC: 2022 Oct 21.
Published in final edited form as: Cell Chem Biol. 2021 May 26;28(10):1501–1513.e5. doi: 10.1016/j.chembiol.2021.05.001

Figure 2. Purified TgASH enzymes exhibit esterase and thioesterase activities.

Figure 2.

(A) Structures of the Quenched fluorogenic Substrate for Esterase (QSE) and thioesterase (QStE) activities for measuring depalmitoylase activity. Quantification of the rate of hydrolysis of (B) QStE and (C) QSE by recombinant TgPPT1, TgASH2, TgASH3 and TgASH4 enzymes. Data represents averages of three independent experiments from three technical triplicates. (D) Schematic of hydrolysis of S-(4-nitrophenyl)thioacetate to release the nitro thiophenol reporter (top) and quantification of the rate of hydrolysis by recombinant TgPPT1, TgASH2, TgASH3 and TgASH4. (E) Schematic showing 4MU_acetate and AMC-acetate (top) and the quantification of the rate of hydrolysis by recombinant TgPPT1, TgASH2, TgASH3 and TgASH4. Data represents averages of three independent experiments from three technical triplicates.