Evidence map›Paper›PMID 33215261›Full record

ArticleApplied microbiology and biotechnology2021

A novel bacterial GH30 xylobiohydrolase from Hungateiclostridium clariflavum.

Katarína Šuchová, Vladimír Puchart, Peter Biely

Abstract read
PubMed Publisher
In one paragraph

Article in Applied microbiology and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.0field-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

6 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Yeast GH30 Xylanase fromMolecules (Basel, Switzerland) · 2022
    Article
  5. Catalytic Diversity of GH30 Xylanases.Molecules (Basel, Switzerland) · 2021
    Article
  6. 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

3 authors at 1 institution in 1 country.

Katarína ŠuchováInstitute of Chemistry, Slovak Academy of Sciences, Dúbravská cesta 9, 845 38, Bratislava, Slovakia. Katarina.Suchova@savba.sk.ORCID http://orcid.org/0000-0001-5529-8383
Vladimír PuchartInstitute of Chemistry, Slovak Academy of Sciences, Dúbravská cesta 9, 845 38, Bratislava, Slovakia.
Peter BielyInstitute of Chemistry, Slovak Academy of Sciences, Dúbravská cesta 9, 845 38, Bratislava, Slovakia.
Institute of Chemistry of the Slovak Academy of Sciences · SK

Funding

Agentúra na Podporu Výskumu a Vývoja APVV-0602-12Vedecká Grantová Agentúra MŠVVaŠ SR a SAV 2/0016/18
6 · The paper itself

Abstract

Typical bacterial GH30 xylanases are glucuronoxylanases requiring 4-O-methylglucuronic acid (MeGlcA) substitution of a xylan main chain for their action. They do not exhibit a significant activity on neutral xylooligosaccharides, arabinoxylan (AraX), or rhodymenan (Rho). In this work, the biochemical characterization of the bacterial Clocl_1795 xylanase from Hungateiclostridium (Clostridium) clariflavum DSM 19732 (HcXyn30A) is presented. Amino acid sequence analysis of HcXyn30A revealed that the enzyme does not contain amino acids known to be responsible for MeGlcA coordination in the -2b subsite of glucuronoxylanases. This suggested that the catalytic properties of HcXyn30A may differ from those of glucuronoxylanases. HcXyn30A shows similar specific activity on glucuronoxylan (GX) and Rho, while the specific activity on AraX is about 1000 times lower. HcXyn30A releases Xyl

Indexed as

Endo-1,4-beta XylanasesXylansAcremoniumEubacterialesOligosaccharidesSubstrate SpecificityEndo-1,4-beta XylanasesOligosaccharidesXylansGlycoside hydrolase family 30Hungateiclostridium clariflavumXylanaseXylobiohydrolaseXylobiose

Identifiers

PMID33215261
OpenAlexW3106212265

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.