Structure of prokaryotic polyamine deacetylase reveals evolutionary functional relationships with eukaryotic histone deacetylases.

@article{Lombardi2011StructureOP,
  title={Structure of prokaryotic polyamine deacetylase reveals evolutionary functional relationships with eukaryotic histone deacetylases.},
  author={Patrick M. Lombardi and Heather D Angell and Douglas A. Whittington and Erin F Flynn and Kanagalaghatta R. Rajashankar and David W Christianson},
  journal={Biochemistry},
  year={2011},
  volume={50 11},
  pages={
          1808-17
        }
}
Polyamines are a ubiquitous class of polycationic small molecules that can influence gene expression by binding to nucleic acids. Reversible polyamine acetylation regulates nucleic acid binding and is required for normal cell cycle progression and proliferation. Here, we report the structures of Mycoplana ramosa acetylpolyamine amidohydrolase (APAH) complexed with a transition state analogue and a hydroxamate inhibitor and an inactive mutant complexed with two acetylpolyamine substrates. The… Expand
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