Evidence map›Paper›PMID 20427274›Full record

ArticleThe Journal of biological chemistry2010

A new archaeal beta-glycosidase from Sulfolobus solfataricus: seeding a novel retaining beta-glycan-specific glycoside hydrolase family along with the human non-lysosomal glucosylceramidase GBA2.

Beatrice Cobucci-Ponzano, Vincenzo Aurilia, Gennaro Riccio, Bernard Henrissat, Pedro M Coutinho, Andrea Strazzulli, Anna Padula, Maria Michela Corsaro, Giuseppina Pieretti, Gabriella Pocsfalvi and 4 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.7field-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

23 citing papers in PubMed, 53 citations in OpenAlex.

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  7. TheThe Journal of biological chemistry · 2020
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  8. Review
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  10. GlcNAc De-Applied and environmental microbiology · 2019
    Article
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  12. Biochemical Characterization of theInternational journal of molecular sciences · 2018
    Article
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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

14 authors at 3 institutions in 2 countries.

Beatrice Cobucci-PonzanoInstitute of Protein Biochemistry, CNR, Via P. Castellino 111, 80131, Naples, Italy.
Vincenzo Aurilia
Gennaro Riccio
Bernard Henrissat
Pedro M Coutinho
Andrea Strazzulli
Anna Padula
Maria Michela Corsaro
Giuseppina Pieretti
Gabriella Pocsfalvi
Immacolata Fiume
Raffaele Cannio
Mosè Rossi
Marco Moracci
Institute of Protein Biochemistry · ITCentre National de la Recherche Scientifique · FRUniversity of Naples Federico II · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbohydrate active enzymes (CAZymes) are a large class of enzymes, which build and breakdown the complex carbohydrates of the cell. On the basis of their amino acid sequences they are classified in families and clans that show conserved catalytic mechanism, structure, and active site residues, but may vary in substrate specificity. We report here the identification and the detailed molecular characterization of a novel glycoside hydrolase encoded from the gene sso1353 of the hyperthermophilic archaeon Sulfolobus solfataricus. This enzyme hydrolyzes aryl beta-gluco- and beta-xylosides and the observation of transxylosylation reactions products demonstrates that SSO1353 operates via a retaining reaction mechanism. The catalytic nucleophile (Glu-335) was identified through trapping of the 2-deoxy-2-fluoroglucosyl enzyme intermediate and subsequent peptide mapping, while the general acid/base was identified as Asp-462 through detailed mechanistic analysis of a mutant at that position, including azide rescue experiments. SSO1353 has detectable homologs of unknown specificity among Archaea, Bacteria, and Eukarya and shows distant similarity to the non-lysosomal bile acid beta-glucosidase GBA2 also known as glucocerebrosidase. On the basis of our findings we propose that SSO1353 and its homologs are classified in a new CAZy family, named GH116, which so far includes beta-glucosidases (EC 3.2.1.21), beta-xylosidases (EC 3.2.1.37), and glucocerebrosidases (EC 3.2.1.45) as known enzyme activities.

Indexed as

beta-GlucosidaseDNA PrimersEscherichia coliGene AmplificationGlucosidasesGlucosylceramidaseHumansKineticsMutagenesis, Site-DirectedOligosaccharidesPhylogenyRecombinant ProteinsSpectrometry, Mass, Electrospray IonizationSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSubstrate SpecificitySulfolobusbeta-GlucosidaseDNA Primersexo-1,4-beta-D-xylosidaseGBA2 protein, humanGlucosidasesGlucosylceramidaseOligosaccharidesRecombinant ProteinsSulfolobus solfataricus beta-glycosidaseXylosidases

Identifiers

PMID20427274
PMCPMC2898359
OpenAlexW2072425060

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.