Lysine deacetylases (KDACs) play critical roles in cell cycle progression, transcriptional regulation, and developmental events, including cardiovascular development and disease and muscular development. In effort to discover what KDAC residues are critical for the activity and stability of the protein, three KDACs were expressed, purified, and found to be active in assays measuring the deacetylation activity. Site-directed mutagenesis was used to introduce an active site histidine to tyrosine mutation in KDAC4 and KDAC7, and as well as combinations with cysteine to alanine mutations in KDAC4. The histidine to tyrosine mutation in both enzymes was determined to be more active by approximately 1000-fold compared to the wild-type enzymes in a commercial assay, whereas the cysteine to alanine mutations reduced activity and stability. Implications for the role of specific residues are discussed.

Molecular substrate interactions of lysine deacetylases

245th National Meeting (2013)

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