Evidence map›Paper›PMID 22012399›Full record

ArticleNature2011

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 and 6 more

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.5field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 97 citations in OpenAlex.

  1. Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026
    Review
  2. Article
  3. Phase Separation and Aggregation of α-Synuclein Diverge at Different Salt Conditions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Zeta-carbonic anhydrases show CSComputational and structural biotechnology journal · 2021
    Article
  8. Article
  9. Hydrogen and Carbon Monoxide-UtilizingFrontiers in microbiology · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Resurrecting ancestral genes in bacteria to interpret ancient biosignatures.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. α-Carbonic Anhydrases Possess Thioesterase Activity.ACS medicinal chemistry letters · 2015
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

16 authors at 4 institutions in 3 countries.

Marjan J SmeuldersDepartment of Microbiology, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ, Nijmegen, The Netherlands.
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
Huub J M Op den Camp
Radboud University Nijmegen · NLMax Planck Society · DEMax Planck Institute for Medical Research · DEPaul Scherrer Institute · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Extremophilic organisms require specialized enzymes for their exotic metabolisms. Acid-loving thermophilic Archaea that live in the mudpots of volcanic solfataras obtain their energy from reduced sulphur compounds such as hydrogen sulphide (H(2)S) and carbon disulphide (CS(2)). The oxidation of these compounds into sulphuric acid creates the extremely acidic environment that characterizes solfataras. The hyperthermophilic Acidianus strain A1-3, which was isolated from the fumarolic, ancient sauna building at the Solfatara volcano (Naples, Italy), was shown to rapidly convert CS(2) into H(2)S and carbon dioxide (CO(2)), but nothing has been known about the modes of action and the evolution of the enzyme(s) involved. Here we describe the structure, the proposed mechanism and evolution of a CS(2) hydrolase from Acidianus A1-3. The enzyme monomer displays a typical β-carbonic anhydrase fold and active site, yet CO(2) is not one of its substrates. Owing to large carboxy- and amino-terminal arms, an unusual hexadecameric catenane oligomer has evolved. This structure results in the blocking of the entrance to the active site that is found in canonical β-carbonic anhydrases and the formation of a single 15-Å-long, highly hydrophobic tunnel that functions as a specificity filter. The tunnel determines the enzyme's substrate specificity for CS(2), which is hydrophobic. The transposon sequences that surround the gene encoding this CS(2) hydrolase point to horizontal gene transfer as a mechanism for its acquisition during evolution. Our results show how the ancient β-carbonic anhydrase, which is central to global carbon metabolism, was transformed by divergent evolution into a crucial enzyme in CS(2) metabolism.

Indexed as

Evolution, MolecularAcidianusCarbon DisulfideCatalytic DomainCrystallography, X-RayHydrolasesModels, MolecularMolecular Sequence DataMutationPhylogenyProtein Structure, TertiaryCarbon DisulfideHydrolases

Identifiers

PMID22012399
OpenAlexW2058987797

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.