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Figure 6
(a) Specific activity of PsEst3 against p-nitrophenol (pNP) esters and fluorescein derivatives. (b) Comparison of the ligand-binding mode. The p-­nitrophenol-bound structure of Est22 (PDB entry 5hc2) and the butyrate-bound structure of thermophilic esterase (PDB entry 4uhf) are superposed on PsEst3 to compare ligand orientations (Huang et al., 2016BB17; Sayer et al., 2015BB38). p-Nitrophenol and butyrate are represented as blue and light green sticks, respectively. Malonate in PsEst3 is shown as relatively thick cyan sticks. The residues that form the binding pocket for an acid are also shown as stick models. The distances between the carbon center of carboxyl group A of malonate and Trp49 and Trp52 are shown as black dotted lines (10.0 and 10.1 Å, respectively). (c) pNP-C2 hydrolysis activity of PsEst3 Ser128 variants. The effects of varying the pH value (d) and organic solvents (e) on PsEst3 activity are shown. pNP-C2 was used as the substrate.

IUCrJ
Volume 10| Part 2| March 2023| Pages 220-232
ISSN: 2052-2525
https://doi.org/10.1107/S2052252523001562