We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
Sandbox Wabash 10 Fumarase
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Fumarase== | ==Fumarase== | ||
| - | <StructureSection load='1stp' size='340' side='right' caption=' | + | <StructureSection load='1stp' size='340' side='right' caption='Unbound Fumarase' 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 | + | 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. |
=='''The Debated Fumarase C Active Site'''== | =='''The Debated Fumarase C Active Site'''== | ||
| Line 22: | Line 22: | ||
== References == | == References == | ||
<ref>PMID: 9098893</ref>. | <ref>PMID: 9098893</ref>. | ||
| + | |||
| + | |||
| + | 129-146, 181-200, and 312-331 | ||
Revision as of 00:18, 29 February 2016
Fumarase
| |||||||||||
References
[1].
129-146, 181-200, and 312-331
