Whittingham, J.L., Turkenburg, J.P., Chandra, S.V., Walsh, M.A. and Grogan, G. (2003) The 2-Å Crystal Structure of 6-Oxo Camphor Hydrolase. Journal Of Biological Chemistry, 278 (3). pp. 1744-1750. ISSN 0021-9258Full text not available from this repository.
6-Oxo camphor hydrolase (OCH) is an enzyme of the crotonase superfamily that catalyzes carbon-carbon bond cleavage in bicyclic beta -diketones via a retro-Claisen reaction (Grogan, G., Roberts, G. A., Bougioukou, D., Turner, N. J., and Flitsch, S. L. (2001) J. Biol. Chem. 276, 12565-12572). The native structure of OCH has been solved at 2.0-Å resolution with selenomethionine multiple wave anomalous dispersion and refined to a final Rfree of 19.0. The structure of OCH consists of a dimer of trimers that resembles the "parent" enzyme of the superfamily, enoyl-CoA hydratase. In contrast to enoyl-CoA hydratase, however, two octahedrally coordinated sodium atoms are found at the 3-fold axis of the hexamer of OCH, and the C-terminal helix of OCH does not form a discrete domain. Models of the substrate, 6-oxo camphor, and a proposed enolate intermediate in the putative active site suggest possible mechanistic roles for Glu-244, Asp-154, His-122, His-45, and His-145.
|Academic Units:||The University of York > Chemistry (York)|
|Depositing User:||York RAE Import|
|Date Deposited:||09 Feb 2009 09:56|
|Last Modified:||09 Feb 2009 10:24|
|Publisher:||The American Society for Biochemistry and Molecular Biology|
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