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Description
Protein post translational modifications are chemical adaptations that take place in the human body to control behavior of proteins. The acetylation of lysine is one type of protein post translational modification. Lysine deacetylases, or KDACs, are enzymes that help regulate proteins by reversing this modification. It has been shown that KDACs are essential in many biological processes. Therefore, better understanding these KDACs could lead to the improved treatment of diseases. Some of the KDACs, including KDAC7, have both a catalytic domain and a second domain of unknown function. The catalytic domain of these KDACs also has a histidine residue at a position that is a tyrosine in other KDACs. We are investigating how these differences from other KDACs affect the activity of KDAC7 with potential substrates. The wild type KDAC7 catalytic domain is considerably less active with model peptide substrates than a KDAC7 mutated to have a tyrosine residue. We are also cloning the full length KDAC7 gene for expression and purification of the full length protein, to measure the effect of the second domain on activity of the catalytic domain. This work will help provide a greater understanding of how KDAC7 interacts with substrates and the possible identity of substrate proteins.
Publication Date
2021
Keywords
Catalytic Specificity, Proteins, Post- translational modification
Disciplines
Chemistry | Physical Sciences and Mathematics
Recommended Citation
Mohammed Gipson, Hajjia S.; Nichols, Kyara A.; Toro, Tasha B.; and Watt, Terry J., "Catalytic Specificity of KDAC 7" (2021). Festival of Scholars. 30.
https://digitalcommons.xula.edu/xula_fos/30