Abstract 1636 Molecular interactions determining the specificity of a lysine deacetylase

Metal-dependent lysine deacetylases (KDACs, also known as histone deacetylases or HDACs) are a family of enzymes responsible for reversing the post-translation modification of lysine acetylation. Because the eleven members of the KDAC family have a conserved catalytic domain structure, the determinants of substrate selectivity for each KDAC are not obvious. Although some acetylated proteins have been associated with particular KDACs as putative substrates, there are few such proteins for which the KDAC responsible for deacetylation has been definitively established.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109912
Primary Topic
Histone Deacetylase Inhibitors Research
Type
article
Field-Weighted Citation Impact
0.00

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article

Abstract 1636 Molecular interactions determining the specificity of a lysine deacetylase

S. B. CARTER, Akila Sridhar, Tasha B. Toro, Terry J. Watt
Journal of Biological Chemistry
Histone Deacetylase Inhibitors Research
article

Abstract 1636 Molecular interactions determining the specificity of a lysine deacetylase

S. B. CARTER, Akila Sridhar, Tasha B. Toro, Terry J. Watt
article en

Abstract

Metal-dependent lysine deacetylases (KDACs, also known as histone deacetylases or HDACs) are a family of enzymes responsible for reversing the post-translation modification of lysine acetylation. Because the eleven members of the KDAC family have a conserved catalytic domain structure, the determinants of substrate selectivity for each KDAC are not obvious. Although some acetylated proteins have been associated with particular KDACs as putative substrates, there are few such proteins for which the KDAC responsible for deacetylation has been definitively established.

Journal of Biological ChemistryVol. 301(5)
University of Georgia (US)
National Institutes of Health, Division of Chemistry
Zero hunger
Openalex Percentile: Top 88%
Histone Deacetylase Inhibitors Research
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