Sandbox Wabash 28 Fumarase
From Proteopedia
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==Theoretical mechanism== | ==Theoretical mechanism== | ||
L-malate is believed to be dehydrated by fumarase into fumarate using basic residues in its active site. | L-malate is believed to be dehydrated by fumarase into fumarate using basic residues in its active site. | ||
| - | [[ | + | [[Image:Fumarase mechanism.jpg|thumb|alt=Fumarase mechanism]] |
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 00:13, 28 February 2016
Fumarase's debated active site
is a highly conserved enzyme found in bacteria as well as mitochondria of eukaryotes which catalyzes the hydration/dehydration of fumarate and L-malate, respectively. The protein, which consists of two dimers laden with α-helices, initially crystalized as a dimer making conclusions about its active site problematic. However, subsequent crystalizations with various inhibitors showed two potential active sites - the locations at which the inhibitors bound: the first discovered theoretical active site is located deep in the interior of the tetramer and was inhibited by pyromelletic acid and citrate - the latter of which is found in the potential active site; β-trimethylsilyl maleate inhibition resulted in the discover of found at the exterior of each subunit. In either case, a basic His residue is believed to be the origin of catalytic function and two such residues were found (His 188 in site A and His 129 in site B). To conclusively determine whether A or B is the active site, site-directed mutagenesis in E. coli was conducted.
Theoretical mechanism
L-malate is believed to be dehydrated by fumarase into fumarate using basic residues in its active site.
