Fig. 1: Deacylase activity profiling of sirtuins.
From: Molecular basis for hierarchical histone de-β-hydroxybutyrylation by SIRT3
a Chemical structures of major lysine acylations. Abbreviations of each acylation mark are used throughout this report. b Domain architectures of human sirtuins and E. coli CobB. NAD+-dependent deacetylase domains are colored in cyan. c Affinity heatmap between histone H31–15K9 acylation peptides and sirtuin proteins. The binding KDs ranging 10−2–10−8 mol/L were transformed into values ranging 2–8 via a -logKD function, and expressed as a linear gradient of red color with annotated affinities. The binding KDs are noted at micromole level in the panel. See also Supplementary Table S1; Fig S2. d Summary of deacylation activities catalyzed by human and E. coli sirtuin proteins. The enzymatic activity is revealed by MALDI-TOF mass spectrometry (MS). See also Supplementary Fig S3. Note: no evidences for Khex, Koct, Kdec, Kdod, Kmyr on endogenous histones have been reported so far and these acylations are synthesized for in vitro study only
