Ph.D., University of California at Berkeley
B.S., University of Kentucky
Area(s) of Interest
Enzyme Structure and Function
Prof. Powers-Lee’s lab studies how protein structures have evolved to catalyze unique enzymatic activities, and to participate in a diverse set of intracellular communications. Her recent studies have been focused on human detoxification of ammonia and its control mechanisms. Carbamoyl phosphate synthetase (CPS), which catalyzes the entry and regulated step of the urea cycle, is known to be the primary site of ammonia detoxification. These studies have utilized structural, biochemical, molecular and bioinformatics techniques to define the structure and function of human CPS and to relate these parameters to those of potential evolutionary relatives. Prof. Powers-Lee’s lab has also reverse engineered various CPSs by creating site-directed mutants, truncated constructions and chimeras. Additionally, studies have been aimed at elucidation of the intramitochondrial environment for CPS and its effect on the enzyme’s structure and function. Applications of these studies include developing treatments for hepatitis and other disorders in which liver function is temporarily or permanently altered.
134 Mugar Life Sciences Building