Cellular and Molecular Life Sciences

, Volume 65, Issue 16, pp 2507–2527

Mechanisms and structures of crotonase superfamily enzymes – How nature controls enolate and oxyanion reactivity


DOI: 10.1007/s00018-008-8082-6

Cite this article as:
Hamed, R.B., Batchelar, E.T., Clifton, I.J. et al. Cell. Mol. Life Sci. (2008) 65: 2507. doi:10.1007/s00018-008-8082-6


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.


Crotonase superfamilyoxyanion holeenolate intermediatescoenzyme Aβ-oxidationproteases

Copyright information

© Birkhaueser 2008

Authors and Affiliations

  1. 1.Chemistry Research Laboratory, Department of ChemistryUniversity of OxfordOxfordUK