Fumarase C (fumarate hydratase) is an enzyme found in eukaryotic cells which catalyzes the reaction between L-malate and fumarate.[1] The catalysis proceeds via the deprotination of the C3 carbon of L-malate, which is followed by the loss of the -OH group attached to the C2 carbon; the intermediate for which is a carbanion transition state.[2] In order for this catalysis to occur L-malate must be bound to fumarase. Studies have determined that fumarase has two carboxylic binding sites (site-A and site-B) which could potentially be the active site for the production of fumarate. However, it has been experimentally determined that binding site-A is in fact the active site of fumarase for the process of converting L-malate to fumarate.
Binding Site Characteristics
Site-A: Site-A can be described as being comprised of atoms from three of the four sub-units (tetramer).
Site-B:
H188N: Effects of Mutation
H188N is used to refer to the fumarase C with five histidines on the C-terminal with histidine 188 mutated to asparagine.
H129N: Effects of Mutation
H129N is used to refer to the fumarase C with five histidines on the C-terminal with histidine 129 mutated to asparagine.
Summary and Conclusions
-Fumarase is a key component in the critic acid cycle
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