This page is for Alex Waters' fumarase page.
Fumarase is a tetrameric enzyme which is responsible for catalyzing the hydration and dehydration of L-malate and fumarate. As an enzyme that has been well characterized in the lab, many crystallographic studies have been done to describe the active site of this enzyme. Several of these studies have been done using inhibitors like pyromellitic acid and beta-trimethylsilyl maleate. These studies produced different results. An area called the "tungsten site", which formed between atoms of three of the four subunits was determined to be the binding site of some of these inhibitors and was called the "A-site". This site exists deep in the enzyme. However, other studies provided data indicating another site, called the "B-site" which also bound the inhibitors and was composed of atoms from one subunit only and is closer to the surface of the enzyme. Both the A-site and the B-Site make use of a Histidine residue to catalyze the reaction. In order to determine the correct active site of fumarase, two mutants were created which altered the histidines responsible for catalyzing the reaction at each site. H188 was expected to change catalytic activity if the A-site was the active site and H129 would change catalytic activity if the B-site was the active site.
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Disease
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Structural highlights
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