Kinetics of Mutations in the and Allosteric Sites of Fumarate Hydratase

Fumarase, also known as fumarate hydratase (FH), is an enzyme that catalyzes the reversible interconversion of fumarate to malate. Fumarase has two sites: active A‐site and allosteric B‐site. Mutations in these sites especially the active site may disrupt the enzyme's efficiency and activity. The main focus of this experiment was characterizing different fumarase mutations in both the active and allosteric sites. The kinetic parameters were determined in both forward and reverse reactions. Some mutants showed a decrease in both K M and V max while others showed an increase in either or both K M and V max . The experimental results suggest that different mutations can have different effects on fumarase efficiency and its overall activity. Further studies are required to address the specific interaction of these mutations involving in those changes in fumarase activity. Support or Funding Information Thanks to the Haines Fund for the Study of Biochemistry at Wabash College. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .