Fumarase (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]
Active Site Characteristics
Active Site-A: Site-A can be described as being comprised of atoms from three of the four sub-units (tetramer).
Active Site-B:
H188N
H188N is used to refer to the fumarase C with five histidines on the C-terminal with histidine 188 mutated to asparagine.
H129N
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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