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. 2024 Nov 3;15:9496. doi: 10.1038/s41467-024-53903-0

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© The Author(s) 2024

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a Pre-screening of selected bacterial deacylases to assess their preferences for different acyl-chain types. A Fluor-de-Lys assay-based screening was performed using histone H3 (APRK_acyl, H3_15-18 or TARK_acyl, H3_6-9), histone H4 (LGK_acyl, H4_10-12), p53 (QPKK_acyl, p53_317-320) and DLAT derived peptide sequences. Depicted is the conversion of peptide in released [AMC] in µM. Positive controls as described in the “Methods” section. The graph depicts the means of both recorded independent replicates (n = 2). Source data are provided as Source Data file. b Michaelis–Menten kinetics for bacterial deacetylases (discontinuous assay). All selected bacterial deacylases showing robust deacetylase activity were summarized (QPKK_ac, p53_317-320). Notably, for RwDmhA (1b), PsApaH (4), and LcApaH (3)/LpApaH (3) we observed substrate inhibition at higher substrate concentration. *: Data adjusted to kinetics with substrate inhibition at high concentration. The experiments were performed in two independent replicates (n = 2). Data are presented as means. Source data are provided as Source Data file. c Michaelis–Menten kinetics for the delactylases VsHdaH (1b) and LcApaH (3). Notably, for VsHdaH (1b) we observed a stereoselectivity toward de-L-lactylation (QPKK_l-la, p53_317-320), while the LcApaH (3) converts both stereoisomers acting as de-d/l-lactylase (LGK_d-la/l-la, H4_10-12). The experiment was done in continuous assay format for VsHdaH (1b) and LcApaH (3). The * indicates the discontinuous assay format used for VsHdaH (1b). The experiments were performed in two independent replicates (n = 2). Data are presented as means. Source data are provided as Source Data file. d Michaelis–Menten kinetics for the deacylase activity for BsAcuC (2c) (continuous assay). BsAcuC (2c) is active as deacetylase, depropionylase, and decrotonylase (LGK_acyl, H4_10-12). The experiments were performed in two independent replicates (n = 2) in a continuous assay format. Data are presented as means. Source data are provided as Source Data file. e Michaelis–Menten kinetics for the deacetylase and depropionylase activity of LpApaH (3) and LcApaH (3) (deactylase: continuous assay format; depropionylase: discontinuous assay format). LpApaH (3) and LcApaH (3) are active deacetylases (LGK_ac, H4_10-12) and depropionylases (QPKK_acyl, p53_317-320). The experiments were performed in two independent replicates (n = 2). Data are presented as means. Source data are provided as Source Data file.