Histone
deacetylases catalyze the hydrolysis of N-acetyl lysine residues in histone
proteins and plays an important role in the regulation of gene expression.
HDACs also deacetylate a growing number of non-histone proteins with
biological importance. We are using a variety of biochemical techniques to
study the chemical mechanism of the metalloenzyme histone deacetylase 8
(HDAC8), as well as characterizing the role of the active site metal.
HDAC Reaction Scheme
Recent
Publications Dowling et al. Structural Studies of
Human Histone Deacetylase 8 and Its Site-Specific Variants Complexed with
Substrate and Inhibitors. Biochemistry (2008) vol. 47 pp.
13554-13563
Gantt et al. Catalytic activity and inhibition of human histone deacetylase
8 is dependent on the identity of the active site metal ion. Biochemistry (2006) vol. 45 pp. 6170-8
Project
Researchers Graduate Students
Sam Gattis
Questions
about this project? Email Sam: sgattis at umich.edu
