Evidence map›Paper›PMID 33446650›Full record

ArticleNature communications2021

Two distinct catalytic pathways for GH43 xylanolytic enzymes unveiled by X-ray and QM/MM simulations.

Mariana A B Morais, Joan Coines, Mariane N Domingues, Renan A S Pirolla, Celisa C C Tonoli, Camila R Santos, Jessica B L Correa, Fabio C Gozzo, Carme Rovira, Mario T Murakami

Abstract read
In one paragraph

Article in Nature communications, 2021. 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
–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

18 citing papers in PubMed.

  1. Article
  2. Genome Assembly and Genomic Characterization ofJournal of fungi (Basel, Switzerland) · 2026
    Article
  3. Whole-genome analysis and enzymatic profiling of Bacillus spizizenii as a xylanase-producing source from Iran.International microbiology : the official journal of the Spanish Society for Microbiology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Harnessing Xylanase Potential inJournal of fungi (Basel, Switzerland) · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Lactate cross-feeding betweenApplied and environmental microbiology · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. 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

10 authors.

Mariana A B MoraisBrazilian Biorenewables National Laboratory (LNBR), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, 13083-100, Brazil.ORCID http://orcid.org/0000-0003-1012-1394
Joan CoinesDepartament de Química Inorgànica i Orgànica & Institut de Química Teórica i Computacional (IQTCUB), Universitat de Barcelona, Barcelona, 08028, Spain.ORCID http://orcid.org/0000-0001-6531-9344
Mariane N DominguesBrazilian Biorenewables National Laboratory (LNBR), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, 13083-100, Brazil.ORCID http://orcid.org/0000-0003-0229-8261
Renan A S PirollaBrazilian Biorenewables National Laboratory (LNBR), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, 13083-100, Brazil.
Celisa C C TonoliBrazilian Biosciences National Laboratory (LNBio), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, 13083-100, Brazil.
Camila R SantosBrazilian Biorenewables National Laboratory (LNBR), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, 13083-100, Brazil.
Jessica B L CorreaBrazilian Biorenewables National Laboratory (LNBR), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, 13083-100, Brazil.
Fabio C GozzoDalton Mass Spectrometry Laboratory, Institute of Chemistry, University of Campinas, Campinas, 13083-970, Brazil.ORCID http://orcid.org/0000-0002-5270-4427
Carme RoviraDepartament de Química Inorgànica i Orgànica & Institut de Química Teórica i Computacional (IQTCUB), Universitat de Barcelona, Barcelona, 08028, Spain. c.rovira@ub.edu.ORCID http://orcid.org/0000-0003-1477-5010
Mario T MurakamiBrazilian Biorenewables National Laboratory (LNBR), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, 13083-100, Brazil. mario.murakami@lnbr.cnpem.br.ORCID http://orcid.org/0000-0002-0405-8010

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Xylanolytic enzymes from glycoside hydrolase family 43 (GH43) are involved in the breakdown of hemicellulose, the second most abundant carbohydrate in plants. Here, we kinetically and mechanistically describe the non-reducing-end xylose-releasing exo-oligoxylanase activity and report the crystal structure of a native GH43 Michaelis complex with its substrate prior to hydrolysis. Two distinct calcium-stabilized conformations of the active site xylosyl unit are found, suggesting two alternative catalytic routes. These results are confirmed by QM/MM simulations that unveil the complete hydrolysis mechanism and identify two possible reaction pathways, involving different transition state conformations for the cleavage of xylooligosaccharides. Such catalytic conformational promiscuity in glycosidases is related to the open architecture of the active site and thus might be extended to other exo-acting enzymes. These findings expand the current general model of catalytic mechanism of glycosidases, a main reaction in nature, and impact on our understanding about their interaction with substrates and inhibitors.

Indexed as

Bacterial ProteinsBinding SitesCatalysisCatalytic DomainCrystallography, X-RayGlycoside HydrolasesKineticsModels, MolecularOligosaccharidesXanthomonasXyloseBacterial ProteinsGlycoside HydrolasesOligosaccharidesXylose

Identifiers

PMID33446650
PMCPMC7809346

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.