Structure of histone deacetylases: insights into substrate recognition and catalysis

Structure. 2001 Dec;9(12):1127-33. doi: 10.1016/s0969-2126(01)00690-6.

Abstract

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.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Catalysis
  • Catalytic Domain
  • Histone Deacetylases / chemistry*
  • Histone Deacetylases / classification
  • Histone Deacetylases / physiology
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Secondary
  • Sequence Homology, Amino Acid
  • Substrate Specificity

Substances

  • Histone Deacetylases