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Journal of Bacteriology, June 2007, p. 4299-4304, Vol. 189, No. 11
0021-9193/07/$08.00+0     doi:10.1128/JB.00198-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Re-Citrate Synthase from Clostridium kluyveri Is Phylogenetically Related to Homocitrate Synthase and Isopropylmalate Synthase Rather Than to Si-Citrate Synthase{dagger} ,{triangledown}

Fuli Li,1 Christoph H. Hagemeier,1 Henning Seedorf,1 Gerhard Gottschalk,2 and Rudolf K. Thauer1*

Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany,1 Göttingen Genomics Laboratory, Institute of Microbiology and Genetics, Georg August University, 37077 Göttingen, Germany2

Received 6 February 2007/ Accepted 19 March 2007

The synthesis of citrate from acetyl-coenzyme A and oxaloacetate is catalyzed in most organisms by a Si-citrate synthase, which is Si-face stereospecific with respect to C-2 of oxaloacetate. However, in Clostridium kluyveri and some other strictly anaerobic bacteria, the reaction is catalyzed by a Re-citrate synthase, whose primary structure has remained elusive. We report here that Re-citrate synthase from C. kluyveri is the product of a gene predicted to encode isopropylmalate synthase. C. kluyveri is also shown to contain a gene for Si-citrate synthase, which explains why cell extracts of the organism always exhibit some Si-citrate synthase activity.

* Corresponding author. Mailing address: Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch-Strasse, D-35043 Marburg, Germany. Phone: 49 6421 178 101. Fax: 49 6421 178 109. E-mail: thauer{at}mpi-marburg.mpg.de

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

{triangledown} Published ahead of print on 30 March 2007.

Journal of Bacteriology, June 2007, p. 4299-4304, Vol. 189, No. 11
0021-9193/07/$08.00+0     doi:10.1128/JB.00198-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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