A covalent succinylcysteine-like intermediate in the enzyme-catalyzed transformation of maleate to fumarate by maleate isomerase.
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.
Fisch
Florian
F
York Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, United Kingdom.
Fleites
Carlos Martinez
CM
Delenne
Marie
M
Baudendistel
Nina
N
Hauer
Bernhard
B
Turkenburg
Johan P
JP
Hart
Sam
S
Bruce
Neil C
NC
Grogan
Gideon
G
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*
D001426:Bacterial Proteins; D005650:Fumarates; D008024:Ligands; D008298:Maleates; C030272:maleic acid; D019745:cis-trans-Isomerases; C108846:maleate isomerase