| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1979174 | Current Opinion in Structural Biology | 2011 | 9 Pages |
Abstract
⺠Histone deacetylases (HDACs) catalyze the hydrolysis of acetyl-l-lysine. ⺠HDACs and related deacetylases adopt the α/β arginase fold. ⺠HDACs employ a promoted-water mechanism for catalysis. ⺠Potent HDAC inhibitors chelate the active site metal ion. ⺠Macrocyclic HDAC inhibitors interact with the mouth of the active site.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Patrick M Lombardi, Kathryn E Cole, Daniel P Dowling, David W Christianson,