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J. Biol. Chem., Vol. 279, Issue 34, 36003-36012, August 20, 2004

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Kinetic and Mechanistic Characterization of the Formyl-CoA Transferase from Oxalobacter formigenes^*

Stefan Jonsson, Stefano Ricagno¶, Ylva Lindqvist¶||, and Nigel G. J. Richards**

From the Department of Chemistry, University of Florida, Gainesville, Florida 32611-7200 and ^¶Molecular Structural Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden

Oxalobacter formigenes is an obligate anaerobe that colonizes the human gastrointestinal tract and employs oxalate breakdown to generate ATP in a novel process involving the interplay of two coupled enzymes and a membrane-bound oxalate:formate antiporter. Formyl-CoA transferase is a critical enzyme in oxalate-dependent ATP synthesis and is the first Class III CoA-transferase for which a high resolution, three-dimensional structure has been determined (Ricagno, S., Jonsson, S., Richards, N., and Lindqvist, Y. (2003) EMBO J. 22, 3210–3219). We now report the first detailed kinetic characterizations of recombinant, wild type formyl-CoA transferase and a number of site-specific mutants, which suggest that catalysis proceeds via a series of anhydride intermediates. Further evidence for this mechanistic proposal is provided by the x-ray crystallographic observation of an acylenzyme intermediate that is formed when formyl-CoA transferase is incubated with oxalyl-CoA. The catalytic mechanism of formyl-CoA transferase is therefore established and is almost certainly employed by all other members of the Class III CoA-transferase family.

Received for publication, May 3, 2004 , and in revised form, June 21, 2004.

The atomic coordinates and structure factors (codes 1VGQ, 1VGR, 1T3Z, and 1T4C) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by National Institutes of Health Grants DK61666 and DK53556 and the Swedish Research Council-Scientific Council for Natural and Engineering Sciences. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

These authors contributed equally to this work.

|| To whom correspondence may be addressed. Fax: 46-8-327626; E-mail: ylva.lindqvist{at}mbb.ki.se. ^** To whom correspondence may be addressed. Fax: 352-392-7918; E-mail: richards{at}qtp.ufl.edu.

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