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. 2022 Jan 10;13:136. doi: 10.1038/s41467-021-27762-y

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a Screening a panel of 32 purified gut microbial β-glucuronidase (GUS) proteins representing seven structural clades using a coupled assay reveals that Loop 1 and FMN-binding GUS orthologs efficiently convert TCS-G to TCS in vitro. b Catalytic efficiency values determined by HPLC further indicate that Loop 1 and FMN-binding GUS orthologs show high TCS-G to TCS-conversion activities in vitro. c Enzymes extracted from human fecal samples exhibit variable TCS-G to TCS turnover rates ex vivo. d The abundance of total bacterial GUS enzymes identified in human fecal samples by activity-based probe-enabled proteomics is correlated with TCS-G turnover rate. e The abundance of Loop 1 GUS proteins identified in human fecal samples by activity-based probe-enabled proteomics, but not other types of GUS, is correlated with TCS-G turnover rate. f Crystal structure of F. prausnitzii 2-L1 (Fp2-L1) GUS with the overall enzyme tetramer shown (purple, gray) and a close-up of the GUSi-glucuronic acid conjugate (green) bound at the enzyme’s active site with the catalytic glutamates highlighted. g TCS-G docked into the active site of Fp2-L1 GUS with residues selected for mutagenesis studies highlighted in cyan. h Catalytic efficiency values of wild-type (WT) and Fp2-L1 GUS mutant proteins. i Crystal structure of Rh3 GUS dimer (green, gray) with FMN bound (highlighted in blue in top monomer). Inset: TCS-G (magenta) was docked using Schrödinger and was found proximal to Y430 and F406 (yellow) at the Rh3 GUS active site (catalytic residues in green). j Catalytic efficiency values for Rh3 GUS mutants showing that the C-terminal domain, Y430 and F406 are important for TCS-G processing. The data are mean ± SEM, n = 3 biological replicates. All statistics were calculated using one-way ANOVA with Tukey’s multiple comparisons test. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001. NA no activity. Source data are provided with this paper. TCS triclosan, TCS-G triclosan-glucuronide, GUS β-glucuronidase.