Sandbox Wabash 27 Fumarase

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 conversion of L-malate to fumarate. Mutations of these sites were performed in order to determine their effects on the enzymatic activity of the fumarases. The results showed that a mutation of site-B lead to no statistical difference in specific activity when compared to wild type activity, while site-A's mutation lead to a significant decrease in enzyme activity. Thus, it was determined that binding site-A is in fact the active site for the conversion of L-malate to fumarate ^[3].

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 acts as an enzymatic catalyst for the production of fumarate from L-malate -

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