Evolution of a new enzyme for carbon disulphide conversion by an acidothermophilic archaeon

Marjan J. Smeulders, Thomas R. M. Barends, Arjan Pol, Anna Scherer, Marcel H. Zandvoort, Anikó Udvarhelyi, Ahmad F. Khadem, Andreas Menzel, John Hermans, Robert L. Shoeman, Hans J. C. T. Wessels, Lambert P. van den Heuvel, Lina Russ, Ilme Schlichting, Mike S. M. Jetten () and Huub J. M. Op den Camp
Additional contact information
Marjan J. Smeulders: Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ
Thomas R. M. Barends: Max-Planck Institute for Medical Research, Jahnstrasse 29
Arjan Pol: Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ
Anna Scherer: Max-Planck Institute for Medical Research, Jahnstrasse 29
Marcel H. Zandvoort: Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ
Anikó Udvarhelyi: Max-Planck Institute for Medical Research, Jahnstrasse 29
Ahmad F. Khadem: Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ
Andreas Menzel: Paul Scherrer Institut
John Hermans: Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ
Robert L. Shoeman: Max-Planck Institute for Medical Research, Jahnstrasse 29
Hans J. C. T. Wessels: Nijmegen Centre for Mitochondrial Disorders, Nijmegen Proteomics Facility, Radboud University Nijmegen Medical Centre, Geert Grooteplein 10PO Box 9101
Lambert P. van den Heuvel: Nijmegen Centre for Mitochondrial Disorders, Nijmegen Proteomics Facility, Radboud University Nijmegen Medical Centre, Geert Grooteplein 10PO Box 9101
Lina Russ: Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ
Ilme Schlichting: Max-Planck Institute for Medical Research, Jahnstrasse 29
Mike S. M. Jetten: Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ
Huub J. M. Op den Camp: Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ

Nature, 2011, vol. 478, issue 7369, 412-416

Abstract: Evolution of novel enzyme activity Many extremophilic organisms require unusual enzymes to help them survive in harsh environments. For example, acid-loving hyperthermophilic Archaea found in the bubbling mud of volcanic solfataras are able to oxidize reduced sulphur compounds. The X-ray crystal structure of a carbon disulphide (CS2) hydrolase from an Acidianus strain isolated from the Solfatara volcano near Naples, Italy, has now been determined. The enzyme, which converts CS2 into hydrogen sulphide and carbon dioxide, has a typical carbonic anhydrase fold and active site, although CO2 is not a substrate for the enzyme. This suggests that CS2 hydrolase is an example of divergent evolution, where a new enzyme has emerged through the evolution of a new quaternary structure rather than through mutations of the active site.

Date: 2011
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DOI: 10.1038/nature10464

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