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Sandbox wabash 04 fumarase
From Proteopedia
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Structure and Function of Fumarase (David Elkins) | Structure and Function of Fumarase (David Elkins) | ||
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | Fumarase is an enzyme that catalyzes the reaction of malate to fumarate, and of fumarate to malate. The fumarase enzyme being observed here is fumarase C, from e. coli. There are two possible active sites that are found in fumarase, both containing carboxylic acid binding sites. These sites are known as the A site and B site. The key residue in both sites is a histidine residue, which can interact with water and can participate in base catalysis. To determine the actual active site of fumarase, Weaver<ref>PMID:9098893</ref>. changed the important histidine residue in each possible active site to an asparagine. <scene name='72/725899/Fumarase_unbound/3'>The residue in Site A was H188, and in Site B the residue was H129N</scene>The experiment measured the specific activity, average activity, and average protein concentration of fumarase upon altering each possible active site individually. The results of the experiment for the mutated fumarase enzymes were compared to that of a wild type enzyme, and the data showed the H129N mutant had similar specific activities to the wild type, but the H188 mutant had a significantly lower specific activity than H129N or wild type. These results show that the active site is the A site because a mutation of H188 yielded significantly reduced enzymatic activity. The mutation of H129N showed small differences in enzymatic activity compared to the wild type fumarase, which further suggests that the B site is not the true active site. <ref>PMID:9098893</ref>. | + | Fumarase is an enzyme that catalyzes the reaction of malate to fumarate, and of fumarate to malate. The fumarase enzyme being observed here is fumarase C, from e. coli. There are two possible active sites that are found in fumarase, both containing carboxylic acid binding sites. These sites are known as the A site and B site. The key residue in both sites is a histidine residue, which can interact with water and can participate in base catalysis. To determine the actual active site of fumarase, Weaver<ref>PMID:9098893</ref>. changed the important histidine residue in each possible active site to an asparagine. <scene name='72/725899/Fumarase_unbound/3'>. The residue in Site A was H188, and in Site B the residue was H129N</scene>The experiment measured the specific activity, average activity, and average protein concentration of fumarase upon altering each possible active site individually. The results of the experiment for the mutated fumarase enzymes were compared to that of a wild type enzyme, and the data showed the H129N mutant had similar specific activities to the wild type, but the H188 mutant had a significantly lower specific activity than H129N or wild type. These results show that the active site is the A site because a mutation of H188 yielded significantly reduced enzymatic activity, <scene name='72/725899/1fur/2'>due to the presence of ASN188 in place of H188</scene>. The mutation of H129N showed small differences in enzymatic activity compared to the wild type fumarase, which further suggests that the B site is not the true active site. <ref>PMID:9098893</ref>. |
== Function == | == Function == | ||
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
| + | <scene name='72/725899/1fur/2'>TextToBeDisplayed</scene> | ||
<scene name='72/725899/Fumarase_unbound/1'>Fumarase (unbound)</scene> | <scene name='72/725899/Fumarase_unbound/1'>Fumarase (unbound)</scene> | ||
Revision as of 02:08, 26 February 2016
Structure and Function of Fumarase (David Elkins)
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References
- ↑ 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
- ↑ 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
[1].
