Evidence map›Paper›PMID 34643018›Full record

ArticleChembiochem : a European journal of chemical biology2022

Defluorination Capability of l-2-Haloacid Dehalogenases in the HAD-Like Hydrolase Superfamily Correlates with Active Site Compactness.

Peter W Y Chan, Nilmadhab Chakrabarti, Chris Ing, Ondrej Halgas, Terence K W To, Marielle Wälti, Alain-Pierre Petit, Christopher Tran, Alexei Savchenko, Alexander F Yakunin and 3 more

Open access · greenAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

18 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Enzymatic carbon-fluorine bond cleavage by human gut microbes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Computational Studies of Enzymes for C-F Bond Degradation and Functionalization.Chemphyschem : a European journal of chemical physics and physical chemistry · 2025
    Review
  8. Article
  9. Journal of the American Chemical Society · 2025
    Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Chemical Diversity and Biosynthesis of Drimane-Type Sesquiterpenes in the Fungal Kingdom.Chembiochem : a European journal of chemical biology · 2022
    Review
  18. Review
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

13 authors at 8 institutions in 3 countries.

Peter W Y ChanDepartment of Biochemistry, University of Toronto, Toronto, Ontario, M5S 1A8, Canada.
Nilmadhab ChakrabartiMolecular Medicine, Hospital for Sick Children, Toronto, Ontario, M5G 1X8, Canada.
Chris IngDepartment of Biochemistry, University of Toronto, Toronto, Ontario, M5S 1A8, Canada.
Ondrej HalgasDepartment of Biochemistry, University of Toronto, Toronto, Ontario, M5S 1A8, Canada.ORCID 0000-0002-2858-9123
Terence K W ToPrincess Margaret Cancer Centre, The Campbell Family Cancer Research Institute, University Health Network, Toronto, Ontario, M5G 1L7, Canada.
Marielle WältiPrincess Margaret Cancer Centre, The Campbell Family Cancer Research Institute, University Health Network, Toronto, Ontario, M5G 1L7, Canada.
Alain-Pierre PetitDepartment of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, M5S 3E5, Canada.
Christopher TranDepartment of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, M5S 3E5, Canada.
Alexei SavchenkoDepartment of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, M5S 3E5, Canada.ORCID 0000-0002-5256-9237
Alexander F YakuninDepartment of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, M5S 3E5, Canada.ORCID 0000-0003-0813-6490
Elizabeth A EdwardsDepartment of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, M5S 3E5, Canada.ORCID 0000-0002-8071-338X
Régis PomèsDepartment of Biochemistry, University of Toronto, Toronto, Ontario, M5S 1A8, Canada.ORCID 0000-0003-3068-9833
Emil F PaiDepartment of Biochemistry, University of Toronto, Toronto, Ontario, M5S 1A8, Canada.ORCID 0000-0002-1162-7242
University of Toronto · CAUniversity Health Network · CABangor University · GBEnvironment and Climate Change Canada · CAHospital for Sick Children · CANational Institutes of Health · USUniversity of Calgary · CAUniversity of Dundee · GB

Funding

The Midwest Center for Structural GenomicsU54GM074942 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ · 2005 to 2009
$51.0M
X-RAY STUDY OF HORMONE-RECEPTOR AND PROTEIN-ANTIBODY COMPLEXESP41RR007707 · NCRR · UNIVERSITY OF CHICAGO · PI YANG, XIANGZHONG · 2002 to 2011
$17.3M
Electric Field-stimulated Protein MechanicsP41GM118217 · NIGMS · UNIVERSITY OF CHICAGO · PI SRAJER, VUKICA · 2019 to 2021
$5.3M
NCRR NIH HHS P41 RR007707NIGMS NIH HHS P41 GM118217NIGMS NIH HHS U54 GM074942
6 · The paper itself

Abstract

l-2-Haloacid dehalogenases, industrially and environmentally important enzymes that catalyse cleavage of the carbon-halogen bond in S-2-halocarboxylic acids, were known to hydrolyse chlorinated, brominated and iodinated substrates but no activity towards fluorinated compounds had been reported. A screen for novel dehalogenase activities revealed four l-2-haloacid dehalogenases capable of defluorination. We now report crystal structures for two of these enzymes, Bpro0530 and Rha0230, as well as for the related proteins PA0810 and RSc1362, which hydrolyse chloroacetate but not fluoroacetate, all at ∼2.2 Å resolution. Overall structure and active sites of these enzymes are highly similar. In molecular dynamics (MD) calculations, only the defluorinating enzymes sample more compact conformations, which in turn allow more effective interactions with the small fluorine atom. Structural constraints, based on X-ray structures and MD calculations, correctly predict the defluorination activity of the homologous enzyme ST2570.

Indexed as

Amino Acid SequenceCrystallography, X-RayHalogenationHydrolasesMolecular Dynamics SimulationProtein ConformationSequence Alignment2-haloacid dehalogenaseHydrolasesenzyme catalysisenzymic defluorinationL-2-haloacid dehalogenasesmolecular dynamicsprotein structures

Identifiers

PMID34643018
PMCPMC10281000
OpenAlexW3206137714

What OpenQuestion holds

Textmetadata
LicenceTDM
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.