Evidence map›Paper›PMID 16609814›Full record

ArticleExtremophiles : life under extreme conditions2006

Characterization of a beta-glycosidase from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius.

Barbara Di Lauro, Mosè Rossi, Marco Moracci

Erratum issuedAbstract read
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In one paragraph

Article in Extremophiles : life under extreme conditions, 2006. 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 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

15 citing papers in PubMed, 34 citations in OpenAlex.

  1. Characterization of a New Glucose-Tolerant GH1 β-Glycosidase fromInternational journal of molecular sciences · 2023
    Article
  2. Article
  3. Release of Soybean Isoflavones by Using a β-Glucosidase from Alicyclobacillus herbarius.Chembiochem : a European journal of chemical biology · 2021
    Article
  4. Review
  5. Article
  6. Glycoside hydrolase gene transcription byBiotechnology for biofuels · 2018
    Article
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Barbara Di LauroInstitute of Protein Biochemistry, Consiglio Nazionale delle Ricerche, Via P. Castellino 111, 80131, Naples, Italy.
Mosè Rossi
Marco Moracci
Institute of Protein Biochemistry · ITConsorzio Roma Ricerche · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In cell free extracts of the thermoacidophilic gram-positive bacterium Alicyclobacillus acidocaldarius ATCC27009, we have identified beta-gluco- and galactosidase activities showing a specific activity of 0.1 and 12 U/mg, respectively. The two enzymatic activities are associated with different polypeptides and we show here the functional cloning, the expression in Escherichia coli and the characterisation of the beta-glucosidase (Aabeta-gly). The enzyme, which is optimally active and stable at temperatures above 65 degrees C, belongs to glycoside hydrolase family 1 (GH1) and shows wide substrate specificity on different aryl-glycosides and cello-oligosaccharides with k (cat)/K (M) for 4-nitrophenyl-beta-D-glucoside and cellobiose of 2,976 and 185 s(-1)mM(-1), respectively. Interestingly, upstream to the beta-glycosidase gene, we identified a second ORF homologous to the ATPase subunit of the bacterial ABC transporters (abc1) that is co-transcribed with the beta-glycosidase gene glyB and that could be involved in the carbohydrate import. The activity of the enzyme on cello-oligosaccharides of up to five glucose units strongly indicates that the enzyme could be involved in vivo in the degradation of glucans together with endoglucanase enzymes previously described. This, together with the co-expression of the two genes, suggests a role for the glyB-abc1 cluster in A. acidocaldarius in the degradation of cellulose and hemicelluloses.

Indexed as

Amino Acid SequenceBacteriaEnzyme StabilityGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicGlucosidasesHydrogen-Ion ConcentrationKineticsMolecular Sequence DataSubstrate SpecificityTemperatureGlucosidases

Identifiers

PMID16609814
OpenAlexW2020005167

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.