Evidence map›Paper›PMID 30850540›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Discovery of novel carbohydrate-active enzymes through the rational exploration of the protein sequences space.

William Helbert, Laurent Poulet, Sophie Drouillard, Sophie Mathieu, Mélanie Loiodice, Marie Couturier, Vincent Lombard, Nicolas Terrapon, Jeremy Turchetto, Renaud Vincentelli and 1 more

Erratum issuedAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
–field-weighted citation impact
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

99 citing papers in PubMed.

  1. Trial
  2. Predicting Functional Diversity Within Enzyme Families: A Practical Perspective.Chembiochem : a European journal of chemical biology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Reverse prediction of carbohydrate esterase polysaccharide targets.Biotechnology for biofuels and bioproducts · 2026
    Article
  7. Generalizable Direct Protein Sequencing With InstaNexus.Molecular & cellular proteomics : MCP · 2026
    Article
  8. Article
  9. BEST: Basic Embedding Search Tool Enhancing Discovery of Novel Enzyme.Interdisciplinary sciences, computational life sciences · 2026
    Article
  10. Article
  11. β-galactanase: an effective tool for the degradation of plant β-ᴅ-galactan.World journal of microbiology & biotechnology · 2025
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Bacterial polysaccharide lyase family 33: Specificity from an evolutionarily conserved binding tunnel.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Article

39 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors.

William HelbertCentre de Recherches sur les Macromolécules Végétales, CNRS, Grenoble Alpes Université, BP53, 38000 Grenoble Cedex 9, France; william.helbert@cermav.cnrs.fr Bernard.Henrissat@afmb.univ-mrs.fr.
Laurent PouletCentre de Recherches sur les Macromolécules Végétales, CNRS, Grenoble Alpes Université, BP53, 38000 Grenoble Cedex 9, France.
Sophie DrouillardCentre de Recherches sur les Macromolécules Végétales, CNRS, Grenoble Alpes Université, BP53, 38000 Grenoble Cedex 9, France.
Sophie MathieuCentre de Recherches sur les Macromolécules Végétales, CNRS, Grenoble Alpes Université, BP53, 38000 Grenoble Cedex 9, France.
Mélanie LoiodiceCentre de Recherches sur les Macromolécules Végétales, CNRS, Grenoble Alpes Université, BP53, 38000 Grenoble Cedex 9, France.
Marie CouturierCentre de Recherches sur les Macromolécules Végétales, CNRS, Grenoble Alpes Université, BP53, 38000 Grenoble Cedex 9, France.
Vincent LombardCNRS, UMR 7257, Université Aix-Marseille, 13288 Marseille, France.
Nicolas TerraponCNRS, UMR 7257, Université Aix-Marseille, 13288 Marseille, France.
Jeremy TurchettoCNRS, UMR 7257, Université Aix-Marseille, 13288 Marseille, France.
Renaud VincentelliCNRS, UMR 7257, Université Aix-Marseille, 13288 Marseille, France.
Bernard HenrissatCNRS, UMR 7257, Université Aix-Marseille, 13288 Marseille, France; william.helbert@cermav.cnrs.fr Bernard.Henrissat@afmb.univ-mrs.fr.ORCID 0000-0002-3434-8588

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Over the last two decades, the number of gene/protein sequences gleaned from sequencing projects of individual genomes and environmental DNA has grown exponentially. Only a tiny fraction of these predicted proteins has been experimentally characterized, and the function of most proteins remains hypothetical or only predicted based on sequence similarity. Despite the development of postgenomic methods, such as transcriptomics, proteomics, and metabolomics, the assignment of function to protein sequences remains one of the main challenges in modern biology. As in all classes of proteins, the growing number of predicted carbohydrate-active enzymes (CAZymes) has not been accompanied by a systematic and accurate attribution of function. Taking advantage of the CAZy database, which groups CAZymes into families and subfamilies based on amino acid similarities, we recombinantly produced 564 proteins selected from subfamilies without any biochemically characterized representatives, from distant relatives of characterized enzymes and from nonclassified proteins that show little similarity with known CAZymes. Screening these proteins for activity on a wide collection of carbohydrate substrates led to the discovery of 13 CAZyme families (two of which were also discovered by others during the course of our work), revealed three previously unknown substrate specificities, and assigned a function to 25 subfamilies.

Indexed as

Carbohydrate MetabolismSequence Analysis, ProteinAmino Acid SequenceAnimalsEnzymesGenomicsHumansPolysaccharidesSequence Analysis, DNAStructure-Activity RelationshipEnzymesPolysaccharidesCAZymespolysaccharidesscreening

Identifiers

PMID30850540
PMCPMC6442616

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.