Article
Unraveling the hidden catalytic activity of vertebrate class IIa histone deacetylases.
Proceedings of the National Academy of Sciences of the United States of America - 30 Oct 2007
Lahm A, Paolini C, Pallaoro M, Nardi M C, Jones P, Neddermann P, Sambucini S, Bottomley M J, Lo Surdo P, Carfí A, Koch U, De Francesco R, Steinkühler C, Gallinari P
Abstract excerpt
Previous findings have suggested that class IIa histone deacetylases (HDACs) (HDAC4, -5, -7, and -9) are inactive on acetylated substrates, thus differing from class I and IIb enzymes. Here, we present evidence supporting this view and demonstrate that class IIa HDACs are very inefficient enzymes on standard substrates. We identified HDAC inhibitors unable to bind recombinant human HDAC4 while showing inhibition...
Topics
- Amino Acid Sequence
- Animals
- Binding Sites
- Catalysis
- Enzyme Activation
- HeLa Cells
- Histidine
- Histone Deacetylases
- Humans
- Models, Molecular
- Mutation
- Protein Structure, Tertiary
- Substrate Specificity