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Sandbox Wabash 22 Fumarase

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== References ==
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Revision as of 00:06, 1 March 2016

Contents

Structure of 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.

Function

Disease

Relevance

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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References

  1. Weaver T, Lees M, Banaszak L. Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site. Protein Sci. 1997 Apr;6(4):834-42. PMID:9098893
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