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Sandbox Wabash 10 Fumarase
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==Fumarase== | ==Fumarase== | ||
<StructureSection load='1stp' size='340' side='right' caption='Unbound Fumarase: highlighting the α-helices (pink), β-sheets (orange), and helical turns in (light blue)' scene='72/726383/Unbound_fumarase/1'> | <StructureSection load='1stp' size='340' side='right' caption='Unbound Fumarase: highlighting the α-helices (pink), β-sheets (orange), and helical turns in (light blue)' scene='72/726383/Unbound_fumarase/1'> | ||
| - | Fumarase C is an enzyme from E. coli (EFumC) that catalyzes the hydration/dehydration reaction between L-malate and fumarate. It catalyzes the hydration of the double bond to form malate. The hydration reaction continues through a carbanion transition state. It has no known metal ion requirement and has a high degree of homology with eukaryotic enzymes. Its homology with cytosolic and mitochondrial enzymes in eukaryotic cells makes it ideal for research. Through x-ray crystallography it has been shown that the enzyme is comprised of a unusual subunit arrangement composed of a core of 20 α-helices, 5 in each of the subunits. | + | Fumarase C is an enzyme from E. coli (EFumC) that catalyzes the hydration/dehydration reaction between L-malate and fumarate. It catalyzes the hydration of the double bond to form malate. The hydration reaction continues through a carbanion transition state. It has no known metal ion requirement and has a high degree of homology with eukaryotic enzymes. Its homology with cytosolic and mitochondrial enzymes in eukaryotic cells makes it ideal for research. Through x-ray crystallography it has been shown that the enzyme is comprised of a unusual subunit arrangement composed of a core of 20 α-helices, 5 in each of the subunits, and it is a tetrameric enzyme with each monomer containing approximately 460 residues. |
=='''The Debated Fumarase C Active Site'''== | =='''The Debated Fumarase C Active Site'''== | ||
Revision as of 00:26, 29 February 2016
Fumarase
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References
[1].
129-146, 181-200, and 312-331
