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Sandbox Wabash 10 Fumarase
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| + | The overall catalytic mechanism of Fumarase drives fumarate formation from L-malate. A water molecule is removed from L-malate to generate fumarate. The first step of this is through a proton removal, and followed by OH- ion removal. The debate for the active site of fumarase is thought to involve two active sites that both contain carboxylic acid binding sites; the A and B site. Biochemical data suggests that the Histidine side chain is one of the bases participating in the catalytic reaction <ref name= "Weaver">PMID:9098893</ref> In order to determine which is the actual active site of fumarase, Weaver <ref name= "Weaver">PMID:9098893</ref> mutated the Histidine side chain, and created two fumarase mutants H129N and H188N. These mutants were developed to hinder the catalytic activity of fumarase. Data was gathered from crystal structure analyses, and activity measurements to confirm the active site <ref name= "Weaver">PMID:9098893</ref>. | ||
| + | <ref name= "Weaver">PMID:9098893</ref> | ||
== Function == | == Function == | ||
Revision as of 02:20, 29 February 2016
Fumarase
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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[1]
