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Journal of Bacteriology, February 2008, p. 1383-1389, Vol. 190, No. 4
0021-9193/08/$08.00+0     doi:10.1128/JB.01593-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

3-Hydroxypropionyl-Coenzyme A Synthetase from Metallosphaera sedula, an Enzyme Involved in Autotrophic CO2 Fixation{triangledown}

Birgit E. Alber,1,2* Johannes W. Kung,1 and Georg Fuchs1

Mikrobiologie, Institut für Biologie II, Albert-Ludwigs-Universität Freiburg, Germany,1 Department of Microbiology, The Ohio State University, 484 West 12th Avenue, Columbus Ohio 432102

Received 1 October 2007/ Accepted 3 December 2007

A modified 3-hydroxypropionate cycle has been proposed as the autotrophic CO2 fixation pathway for the thermoacidophilic crenarchaeon Metallosphaera sedula. The cycle requires the reductive conversion of 3-hydroxypropionate to propionyl-coenzyme A (propionyl-CoA). The specific activity of the 3-hydroxypropionate-, CoA-, and MgATP-dependent oxidation of NADPH in autotrophically grown cells was 0.023 µmol min–1mg protein–1. The reaction sequence is catalyzed by at least two enzymes. The first enzyme, 3-hydroxypropionyl-CoA synthetase, catalyzes the following reaction: 3-hydroxypropionate + ATP + CoA -> 3-hydroxypropionyl-CoA + AMP + PPi. The enzyme was purified 95-fold to a specific activity of 18 µmol min–1 mg protein–1 from autotrophically grown M. sedula cells. An internal peptide sequence was determined and a gene encoding a homologous protein identified in the genome of Sulfolobus tokodaii; similar genes were found in S. solfataricus and S. acidocaldarius. The gene was heterologously expressed in Escherichia coli, and the His-tagged protein was purified. Both the native enzyme from M. sedula and the recombinant enzyme from S. tokodaii not only activated 3-hydroxypropionate to its CoA ester but also activated propionate, acrylate, acetate, and butyrate; however, with the exception of propionate, the affinities for these substrates were reduced. 3-Hydroxypropionyl-CoA synthetase is up-regulated eightfold in autotrophically versus heterotrophically grown M. sedula, supporting its proposed role during CO2 fixation in this archaeon and possibly other members of the Sulfolobaceae family.

* Corresponding author. Mailing address: Department of Microbiology, The Ohio State University, 484 West 12th Avenue, Columbus OH 43210-1292. Phone: (614) 247-4443. Fax: (614) 292-8120. E-mail: alber.8{at}osu.edu

{triangledown} Published ahead of print on 28 December 2007.

Journal of Bacteriology, February 2008, p. 1383-1389, Vol. 190, No. 4
0021-9193/08/$08.00+0     doi:10.1128/JB.01593-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Kockelkorn, D., Fuchs, G. (2009). Malonic Semialdehyde Reductase, Succinic Semialdehyde Reductase, and Succinyl-Coenzyme A Reductase from Metallosphaera sedula: Enzymes of the Autotrophic 3-Hydroxypropionate/4-Hydroxybutyrate Cycle in Sulfolobales. J. Bacteriol. 191: 6352-6362 [Abstract] [Full Text]  
  • Teufel, R., Kung, J. W., Kockelkorn, D., Alber, B. E., Fuchs, G. (2009). 3-Hydroxypropionyl-Coenzyme A Dehydratase and Acryloyl-Coenzyme A Reductase, Enzymes of the Autotrophic 3-Hydroxypropionate/4-Hydroxybutyrate Cycle in the Sulfolobales. J. Bacteriol. 191: 4572-4581 [Abstract] [Full Text]  
  • Ramos-Vera, W. H., Berg, I. A., Fuchs, G. (2009). Autotrophic Carbon Dioxide Assimilation in Thermoproteales Revisited. J. Bacteriol. 191: 4286-4297 [Abstract] [Full Text]  


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