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Journal of Bacteriology, September 2006, p. 6460-6468, Vol. 188, No. 18
0021-9193/06/$08.00+0     doi:10.1128/JB.00659-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Properties of Succinyl-Coenzyme A:D-Citramalate Coenzyme A Transferase and Its Role in the Autotrophic 3-Hydroxypropionate Cycle of Chloroflexus aurantiacus

Silke Friedmann, Birgit E. Alber, and Georg Fuchs*

Mikrobiologie, Institut Biologie II, Universität Freiburg, Freiburg, Germany

Received 9 May 2006/ Accepted 5 July 2006

The phototrophic bacterium Chloroflexus aurantiacus uses the 3-hydroxypropionate cycle for autotrophic CO2 fixation. This cycle starts with acetyl-coenzyme A (CoA) and produces glyoxylate. Glyoxylate is an unconventional cell carbon precursor that needs special enzymes for assimilation. Glyoxylate is combined with propionyl-CoA to ß-methylmalyl-CoA, which is converted to citramalate. Cell extracts catalyzed the succinyl-CoA-dependent conversion of citramalate to acetyl-CoA and pyruvate, the central cell carbon precursor. This reaction is due to the combined action of enzymes that were upregulated during autotrophic growth, a coenzyme A transferase with the use of succinyl-CoA as the CoA donor and a lyase cleaving citramalyl-CoA to acetyl-CoA and pyruvate. Genomic analysis identified a gene coding for a putative coenzyme A transferase. The gene was heterologously expressed in Escherichia coli and shown to code for succinyl-CoA:D-citramalate coenzyme A transferase. This enzyme, which catalyzes the reaction D-citramalate + succinyl-CoA -> D-citramalyl-CoA + succinate, was purified and studied. It belongs to class III of the coenzyme A transferase enzyme family, with an aspartate residue in the active site. The homodimeric enzyme composed of 44-kDa subunits was specific for succinyl-CoA as a CoA donor but also accepted D-malate and itaconate instead of D-citramalate. The CoA transferase gene is part of a cluster of genes which are cotranscribed, including the gene for D-citramalyl-CoA lyase. It is proposed that the CoA transferase and the lyase catalyze the last two steps in the glyoxylate assimilation route.

* Corresponding author. Mailing address: Mikrobiologie, Institut Biologie II, Schänzlestr. 1, D-79104 Freiburg, Germany. Phone: (49) 761-2032649. Fax: (49) 761-2032626. E-mail: georg.fuchs{at}biologie.uni-freiburg.de.

Journal of Bacteriology, September 2006, p. 6460-6468, Vol. 188, No. 18
0021-9193/06/$08.00+0     doi:10.1128/JB.00659-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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