Ontology highlight
ABSTRACT:
SUBMITTER: Lahm A
PROVIDER: S-EPMC2077257 | biostudies-literature | 2007 Oct
REPOSITORIES: biostudies-literature
Lahm A A Paolini C C Pallaoro M M Nardi M C MC Jones P P Neddermann P P Sambucini S S Bottomley M J MJ Lo Surdo P P Carfí A A Koch U U De Francesco R R Steinkühler C C Gallinari P P
Proceedings of the National Academy of Sciences of the United States of America 20071023 44
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 in a typical HDAC4 enzymatic assay, suggesting that the observed activity rather ref ...[more]