title: A covalent succinylcysteine-like intermediate in the enzyme-catalyzed transformation of maleate to fumarate by maleate isomerase.
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.
authors.affiliation: York Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, United Kingdom.
authors.forename: Florian
authors.initials: F
authors.lastname: Fisch
authors.forename: Carlos Martinez
authors.initials: CM
authors.lastname: Fleites
authors.forename: Marie
authors.initials: M
authors.lastname: Delenne
authors.forename: Nina
authors.initials: N
authors.lastname: Baudendistel
authors.forename: Bernhard
authors.initials: B
authors.lastname: Hauer
authors.forename: Johan P
authors.initials: JP
authors.lastname: Turkenburg
authors.forename: Sam
authors.initials: S
authors.lastname: Hart
authors.forename: Neil C
authors.initials: NC
authors.lastname: Bruce
authors.forename: Gideon
authors.initials: G
authors.lastname: Grogan
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D055162:Biocatalysis; D005650:Fumarates / Q000138:chemical synthesis* / Q000737:chemistry; D008024:Ligands; D008298:Maleates / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D013237:Stereoisomerism; D019745:cis-trans-Isomerases / Q000737:chemistry / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D005650:Fumarates; D008024:Ligands; D008298:Maleates; C030272:maleic acid; D019745:cis-trans-Isomerases; C108846:maleate isomerase