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 β-diketones and C-C bond formation, cleavage and oxidation. CS enzymes possess a canonical fold formed from repeated ββα units that assemble into two approximately perpendicular β-sheets surrounded by α-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.
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R. B. Hamed, E. T. Batchelar: These authors contributed equally to this work.
Received 18 January 2008; received after revision 25 March 2008; accepted 1 April 2008
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Hamed, R.B., Batchelar, E.T., Clifton, I.J. et al. Mechanisms and structures of crotonase superfamily enzymes – How nature controls enolate and oxyanion reactivity. Cell. Mol. Life Sci. 65, 2507–2527 (2008). https://doi.org/10.1007/s00018-008-8082-6
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DOI: https://doi.org/10.1007/s00018-008-8082-6