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Originally published In Press as doi:10.1074/jbc.M011538200 on January 16, 2001

J. Biol. Chem., Vol. 276, Issue 16, 12565-12572, April 20, 2001
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The Desymmetrization of Bicyclic beta -Diketones by an Enzymatic Retro-Claisen Reaction
A NEW REACTION OF THE CROTONASE SUPERFAMILY*

Gideon GroganDagger , Gareth A. RobertsDagger , Despina Bougioukou, Nicholas J. Turner, and Sabine L. Flitsch§

From the Edinburgh Centre for Protein Technology, Department of Chemistry, University of Edinburgh, The King's Buildings, West Mains Road, Edinburgh EH9 3JJ, United Kingdom

The enzyme 6-oxocamphor hydrolase, which catalyzes the desymmetrization of 6-oxocamphor to yield (2R,4S)-alpha -campholinic acid, has been purified with a factor of 35.7 from a wild type strain of Rhodococcus sp. NCIMB 9784 grown on (1R)-(+)-camphor as the sole carbon source. The enzyme has a subunit molecular mass of 28,488 Da by electrospray mass spectrometry and a native molecular mass of ~83,000 Da indicating that the active protein is trimeric. The specific activity was determined to be 357.5 units mg-1, and the Km was determined to be 0.05 mM for the natural substrate. The N-terminal amino acid sequence was obtained from the purified protein, and using this information, the gene encoding the enzyme was cloned. The translation of the gene was found to bear significant homology to the crotonase superfamily of enzymes. The gene is closely associated with an open reading frame encoding a ferredoxin reductase that may be involved in the initial step in the biodegradation of camphor. A mechanism for 6-oxocamphor hydrolase based on sequence homology and the known mechanism of the crotonase enzymes is proposed.

* This work was supported by funds from the Biotechnology Biosciences Research Council (to G. G. and G. A. R.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF323755.

Dagger These authors contributed equally to this work.

§ To whom correspondence should be addressed. Tel.: 44-131-650-4737; Fax: 44-131-650-4743; E-mail: s.flitsch@ed.ac.uk; Internet: http://www.ed.ac.uk/~slf10.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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