Evidence map›Paper›PMID 19053248›Full record

ArticleBiochemistry2008

Functional proteomic and structural insights into molecular recognition in the nitrilase family enzymes.

Katherine T Barglow, Kumar S Saikatendu, Michael H Bracey, Ruth Huey, Garrett M Morris, Arthur J Olson, Raymond C Stevens, Benjamin F Cravatt

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 60 citations in OpenAlex.

  1. Crystal structure of carbon-nitrogen hydrolase from Helicobacter pylori G27.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Nit1 is a metabolite repair enzyme that hydrolyzes deaminated glutathione.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Article
  11. Article
  12. Review
  13. Target deconvolution techniques in modern phenotypic profiling.Current opinion in chemical biology · 2013
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Hits, Fhits and Nits: beyond enzymatic function.Advances in enzyme regulation · 2011
    Review
  19. Article
  20. 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

8 authors at 1 institution in 1 country.

Katherine T BarglowThe Skaggs Institute for Chemical Biology and Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
Kumar S Saikatendu
Michael H Bracey
Ruth Huey
Garrett M Morris
Arthur J Olson
Raymond C Stevens
Benjamin F Cravatt
Scripps Research Institute · US

Funding

AutoDock Suite: Next Generation Environment for Drug DesignR01GM069832 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI FORLI, STEFANO · 2004 to 2025
$10.9M
Chemical Approaches for Activity-Based ProteomicsR37CA087660 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI CRAVATT, BENJAMIN F · 2009 to 2018
$3.1M
CHEMICAL APPROACHES FOR ACTIVITY BASED PROTEOMICSR01CA087660 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI CRAVATT, BENJAMIN F · 2000 to 2008
$2.8M
A Computational Docking Resource for Cancer ResearchR24CA095830 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI OLSON, ARTHUR J. · 2002 to 2006
$1.5M
Howard Hughes Medical InstituteNCI NIH HHS CA087660NCI NIH HHS R01 CA087660NCI NIH HHS R24 CA095830NCI NIH HHS R24-CA095830NCI NIH HHS R37 CA087660NIGMS NIH HHS R01 GM069832NIGMS NIH HHS R01-GM069832
6 · The paper itself

Abstract

Nitrilases are a large and diverse family of nonpeptidic C-N hydrolases. The mammalian genome encodes eight nitrilase enzymes, several of which remain poorly characterized. Prominent among these are nitrilase-1 (Nit1) and nitrilase-2 (Nit2), which, despite having been shown to exert effects on cell growth and possibly serving as tumor suppressor genes, are without known substrates or selective inhibitors. In previous studies, we identified several nitrilases, including Nit1 and Nit2, as targets for dipeptide-chloroacetamide activity-based proteomics probes. Here, we have used these probes, in combination with high-resolution crystallography and molecular modeling, to systematically map the active site of Nit2 and identify residues involved in molecular recognition. We report the 1.4 A crystal structure of mouse Nit2 and use this structure to identify residues that discriminate probe labeling between the Nit1 and Nit2 enzymes. Interestingly, some of these residues are conserved across all vertebrate Nit2 enzymes and, conversely, not found in any vertebrate Nit1 enzymes, suggesting that they are key discriminators of molecular recognition between these otherwise highly homologous enzymes. Our findings thus point to a limited set of active site residues that establish distinct patterns of molecular recognition among nitrilases and provide chemical probes to selectively perturb the function of these enzymes in biological systems.

Indexed as

Amino Acid SequenceAminohydrolasesAnimalsCrystallography, X-RayLiverMiceModels, MolecularMolecular ConformationMolecular Sequence DataProtein ConformationProtein Structure, TertiaryProteomicsSequence Homology, Amino AcidAminohydrolasesnitrilase

Identifiers

PMID19053248
PMCPMC2665915
OpenAlexW2028400606

What OpenQuestion holds

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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.