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Sandbox Wabash 22 Fumarase
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Mutations of Fumarase--Mazin Hakim
Fumarase C is an important enzyme that catalyzes the hydration and dehydration equilibrium between L-malate and fumarate. Fumarase C from E.coli is highly homologous with the same enzyme from eukaryotes, and therefore is a prime analyte for the study of its reaction mechanism. In the study, "Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site"[1] conducted by Weaver et. al., there are various points of interest to address. these include the structure of the fumarase active site, what amino acids are present there, and free energy of the intermediate, but also extend to a discussion about the two possible locations of the active site and how this true active side was determined via a mutations and collection of data.
Possible Locations of the Active Site
The structure of the active site that is thought to consist of the overall catalytic process are the two basic groups, one responsible for deprotinating L-malate (B1) and another responsible for the removal of -OH from L-malate to form a water. Upon further crystallographic studies, there were two different active sites found, one that was a 3 subunit binding site, the A site, of inhibitors citrate and pyromellitic acid and another single subunit labeled the B site.
Structure of the Active Site
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