An active site tyrosine residue is essential for amidohydrolase but not for esterase activity of a class 2 histone deacetylase-like bacterial enzyme.

@article{Moreth2007AnAS,
  title={An active site tyrosine residue is essential for amidohydrolase but not for esterase activity of a class 2 histone deacetylase-like bacterial enzyme.},
  author={Kristin Moreth and Daniel Riester and C. Hildmann and Ren{\'e} Hempel and Dennis Wegener and Andreas Schober and Andreas Schwienhorst},
  journal={The Biochemical journal},
  year={2007},
  volume={401 3},
  pages={
          659-65
        }
}
HDACs (histone deacetylases) are considered to be among the most important enzymes that regulate gene expression in eukaryotic cells acting through deacetylation of epsilon-acetyl-lysine residues within the N-terminal tail of core histones. In addition, both eukaryotic HDACs as well as their bacterial counterparts were reported to also act on non-histone targets. However, we are still far from a comprehensive understanding of the biological activities of this ancient class of enzymes. In the… CONTINUE READING
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