Fumarase C from E.coli is an enzyme that catalyzes the reversible hydration/dehydration reaction between the metabolites L-malate and fumarate. Fumarase C is an enzyme found in a large variety of organisms namely eukaryotes, bacteria, yeast, molds, plants, invertebrates, and mammals (Hill, & Teipel, 1971). Due to the enzymes similarity with eukaryotic Fumarases, it has been much easier to characterize and understand its mechanisms. However, the true active site of Fumarase has been up for much debate.
Two sites have been identified as the possible active sites of Fumarase C in E coli, they are designated as the A-site and B-site. The A-site was initially considered as the active site for a couple reasons, 1) the active site of fumarase has never been described as monomeric (which the A-site is has multi-subunits), 2) a well known active-site inhibitor of fumarase C known as Citrate, through experiments was logistically found near the A-site of the enzyme. However, the A-site is found in a deep pit of the enzyme and with an unusual water attached. His188, a side-chain found in the A-site was observed interacting with the water, and also observed hydrogen-bonding with an oxygen atom belonging to our citrate that was mentioned earlier. At the same time however, there was speculation that the active site of Fumarase C may exist at the B site because its closer to the surface of the enzyme.
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