Fig. 2: Pre-screening of bacterial deacylases for lysine deacylase and polyamine deacylase activity.

a Activity of bacterial deacylases toward Boc-Lys(Ac)-AMC. HsHDAC6 (1g) was used as reference. The enzymes VsHdaH (1b), BsAcuC (2c) and LcApaH (3) and LpApaH (3) are active in deacetylating Boc-Lys(Ac)-AMC. The catalytic inactive mutants were analyzed as controls. The experiments were performed in three replicates. Bars depict means ± standard deviation (SD). Significance was tested by unpaired, two-tailed t-tests (p < 0.05) (n = 3) either to the catalytically inactive mutant or to HsHDAC6. Exact values can be found in the Source Data. Source data are provided as Source Data file. b Fluor-de-Lys Peptide 2 is deacetylated by BsAcuC (2c), by LcApaH (3) and by LpApaH (3). As references, we show HDAC1 (2a; class I), HDAC8 (2a; class I), and HDAC6 (1 g; class IIb) are competent to deacetylate peptide 2. The inactivity of the catalytic inactive mutants confirms an enzymatic reaction as indicated. The experiments were performed in three replicates. Bars depict means ± SD. Significance was tested by unpaired, two-tailed t-tests (p < 0.05) (n = 3) either to the catalytically inactive mutant or to HsHDAC6. Exact values can be found in the Source Data. Source data are provided as Source Data file. c Fluor-de-Lys reporter peptide 2a is deacetylated by various bacterial enzymes. We observed the strongest activity for the cluster 1b enzymes KpHdaH (1b) and VsHdaH (1b) and for PsApaH (4) of cluster 4. Moderate activity is also observed for BsAcuC (2c) and for the enzymes LpApaH (3) and LcApaH (3). The catalytic inactive mutants confirm the enzymatic reactions. The experiments were performed in three replicates (n = 3), except for human HDAC6 (n = 1), HDAC7 (n = 2), and HDAC8 (n = 2). Bars depict means ± SD. Significance was tested by t-tests (p < 0.05) to catalytically inactive mutant or to HsHDAC9. Exact values can be found in the Source Data. Source data are provided as Source Data file. d Cluster 4 contains active polyamine deacetylases. PsApaH (4) is active in deacetylating the polyamines N¹-acetylputrescine, N¹-acetylcadaverine, N¹-acetylspermine, N¹,N¹²-diacetylspermine with similar efficiency. PsApaH (4) weakly deacetylates N⁸-acetylspermidine. The catalytic inactive mutants confirm an enzymatic reaction. As control, we used the P. aeruginosa enzyme PA1409. The experiments were performed in three replicates (n = 3). Bars depict means ± SD. Source data are provided as Source Data file.