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Cell Mol Life Sci ; 65(16): 2507-27, 2008 Aug.
Article in English | MEDLINE | ID: mdl-18470480

ABSTRACT

Structural and mechanistic studies on the crotonase superfamily (CS) are reviewed with the aim of illustrating how a conserved structural platform can enable catalysis of a very wide range of reactions. Many CS reactions have precedent in the 'carbonyl' chemistry of organic synthesis; they include alkene hydration/isomerization, aryl-halide dehalogenation, (de)carboxylation, CoA ester and peptide hydrolysis, fragmentation of beta-diketones and C-C bond formation, cleavage and oxidation. CS enzymes possess a canonical fold formed from repeated betabetaalpha units that assemble into two approximately perpendicular beta-sheets surrounded by alpha-helices. CS enzymes often, although not exclusively, oligomerize as trimers or dimers of trimers. Two conserved backbone NH groups in CS active sites form an oxyanion 'hole' that can stabilize enolate/oxyanion intermediates. The range and efficiency of known CS-catalyzed reactions coupled to their common structural platforms suggest that CS variants may have widespread utility in biocatalysis.


Subject(s)
Carboxylic Acids/metabolism , Enoyl-CoA Hydratase/chemistry , Enoyl-CoA Hydratase/metabolism , Nature , Amino Acid Sequence , Animals , Binding Sites , Humans , Molecular Sequence Data , Protein Structure, Quaternary , Protein Structure, Secondary
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