According to the Centers for Disease Control and Prevention, one-fourth of the world’s population is infected with Tuberculosis (TB). KatG is an enzyme responsible for the activation of the pro-drug isoniazid which treats TB. Patrick Sahrmann, a junior majoring in Biochemistry, is investigating the role of a specific amino acid (M377) by studying a corresponding mutated version of the protein.
For his approach, Sahrmann performed a series of kinetic studies on the mutated protein for comparison to that of the normal enzyme. Since KatG converts H2O2 to O2 in its catalytic pathway, an oxygen-sensitive electrode was used to measure substrate conversion.
As a result of Sahrmann’s study, Sahrmann discovered the mutated protein displays similar kinetic parameters to that of a wild-type but becomes inactive after fewer substrate turnovers. This suggests that while M377 is not directly related to catalase turnover, it is necessary for mechanisms of catalytic recovery from oxidized protein.
Sahrmann said his undergraduate research experience with his mentor, Dr. Douglas Goodwin, has solidified his decision to pursue enzymology research in graduate school, specifically through a biophysical lens.
Sahrmann has been awarded the Marks Family Scholarship for Undergraduate Research and presented his research at the 2018 Southeast Enzyme Conference in Atlanta, Georgia, earlier this month.
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