Sandbox Wabash 26 Fumarase

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This page is for Alex Water's fumarase page.
This page is for Alex Water's fumarase page.
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You fault text for your page '''Sandbox Wabash 26 Fumarase'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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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". However
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== Function ==
== Function ==

Revision as of 16:55, 28 February 2016

Mutations of Fumarase

Caption for this structure

Drag the structure with the mouse to rotate

References

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