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From the same journal

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

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Published copy (DOI)

Author(s)

  • Florian Fisch
  • Carlos Martinez Fleites
  • Marie Delenne
  • Nina Baudendistel
  • Bernhard Hauer
  • Johan P. Turkenburg
  • Sam Hart
  • Neil C. Bruce
  • Gideon Grogan

Department/unit(s)

Publication details

JournalJournal of the American Chemical Society
DatePublished - 25 Aug 2010
Issue number33
Volume132
Number of pages3
Pages (from-to)11455-11457
Original languageEnglish

Abstract

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.

    Research areas

  • CIS-TRANS ISOMERASE, SUBTILIS GLUTAMATE RACEMASE, ARYLMALONATE DECARBOXYLASE, CRYSTAL-STRUCTURE, ESCHERICHIA-COLI, MECHANISM, EVOLUTION, CLONING, ACID

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