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A Covalent Succinylcysteine-like Intermediate in the Enzyme-Catalyzed Transformation of Maleate to Fumarate by Maleate Isomerase

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journal contribution
posted on 25.08.2010, 00:00 by Florian Fisch, Carlos Martinez Fleites, Marie Delenne, Nina Baudendistel, Bernhard Hauer, Johan P. Turkenburg, Sam Hart, Neil C. Bruce, Gideon Grogan
Maleate isomerase (MI), a member of the Asp/Glu racemase superfamily, catalyzes cis−trans isomerization of the C2−C3 double bond in maleate to yield fumarate. Mutational studies, in conjunction with the structure of the C194A mutant of Nocardia farcinica MI cocrystallized with maleate, have revealed an unprecedented mode of catalysis for the superfamily in which the isomerization reaction is initiated by nucleophilic attack of cysteine at the double bond, yielding a covalent succinylcysteine-like intermediate.

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