Structure of histone deacetylases: insights into substrate recognition and catalysis.
Histone deacetylases catalyze the removal of the acetyl moiety from acetyl-lysine within histones to promote gene repression and silencing. These enzymes fall into distinct families based on primary sequence homology and functional properties in vivo. Recent structural studies of histone deacetylases and their homologs from bacteria have provided important insights into the mode of substrate recognition and catalysis by these enzymes.
Marmorstein
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The Wistar Institute and the Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, USA. marmor@wistar.upenn.edu
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D020134:Catalytic Domain; D006655:Histone Deacetylases / Q000737:chemistry* / Q000145:classification / Q000502:physiology; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D006655:Histone Deacetylases