Sandbox Wabash 09 Fumarase

<StructureSection load='1YFE_mm1.pdb' size='340' side='right' caption='Quaternary Structure of Fumarase (provided by Dr. Taylor)' scene=''>

<StructureSection load='1YFE_mm1.pdb' size='340' side='right' caption='Quaternary Structure of Fumarase (provided by Dr. Taylor)' scene=''>

Fumarase C, which is found in E. coli, is a enzyme homologous with some eurkaryotic enzymes found in both the cytosol and mitochondria. Fumarase catalyzes the dehydration of L-malate to form fumarate, as well as the reverse hydration reaction. Two basic groups play a role in the overall catalytic process of fumarase. The first basic group is responsible for the removal of a proton from the C3 carbon of L-malate, forming a carbanion. The carbanion is stabilized by an aci-carobxylate intermediate which is formed at C4. The carboxyl group on C4 has a negative two formal charge, stabilizing the substrate after the removal of the proton. The second basic group is protonated, for the creation of fumarate, and leads to the formation of a water molecule as a hydroxyl group is removed from C2. Interestingly, fumarase contains two possible sites at which catalysis occurs, prompting researchers to determine which of the sites is the true active site of the enzyme<ref>Weaver T, Lees M, Banaszak L. 1997. Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site. Protein Science 6:834-842.ref>.

Fumarase C, which is found in E. coli, is a enzyme homologous with some eurkaryotic enzymes found in both the cytosol and mitochondria. Fumarase catalyzes the dehydration of L-malate to form fumarate, as well as the reverse hydration reaction. Two basic groups play a role in the overall catalytic process of fumarase. The first basic group is responsible for the removal of a proton from the C3 carbon of L-malate, forming a carbanion. The carbanion is stabilized by an aci-carobxylate intermediate which is formed at C4. The carboxyl group on C4 has a negative two formal charge, stabilizing the substrate after the removal of the proton. The second basic group is protonated, for the creation of fumarate, and leads to the formation of a water molecule as a hydroxyl group is removed from C2. Interestingly, fumarase contains two possible sites at which catalysis occurs, prompting researchers to determine which of the sites is the true active site of the enzyme<ref>Weaver T, Lees M, Banaszak L. 1997. Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site. Protein Science 6:834-842.ref>.

== Determining the Active Site ==

== Determining the Active Site ==