Evidence map›Paper›PMID 31300677›Full record

ArticleScientific reports2019

GeneHunt for rapid domain-specific annotation of glycoside hydrolases.

S N Nguyen, A Flores, D Talamantes, F Dar, A Valdez, J Schwans, R Berlemont

Abstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Harnessing the sponge microbiome for industrial biocatalysts.Applied microbiology and biotechnology · 2020
    Review
  12. 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

7 authors.

S N NguyenDepartment of Biological Sciences, California State University Long Beach, Long Beach, California, USA.
A FloresDepartment of Biological Sciences, California State University Long Beach, Long Beach, California, USA.
D TalamantesDepartment of Biological Sciences, California State University Long Beach, Long Beach, California, USA.
F DarDepartment of Biological Sciences, California State University Long Beach, Long Beach, California, USA.
A ValdezDepartment of Biological Sciences, California State University Long Beach, Long Beach, California, USA.
J SchwansDepartment of Chemistry and Biochemistry, California State University Long Beach, Long Beach, California, USA.
R BerlemontDepartment of Biological Sciences, California State University Long Beach, Long Beach, California, USA. Renaud.berlemont@csulb.edu.

Funding

CSULB Building Biomedical Research Program: Overall ComponentUL1GM118979 · NIGMS · CALIFORNIA STATE UNIVERSITY LONG BEACH · PI CHUN, CHI-AH, DILLON, JESSE · 2015 to 2023
$20.7M
Research Initiative for Scientific Enhancement at CSULBR25GM071638 · NIGMS · CALIFORNIA STATE UNIVERSITY LONG BEACH · PI BUONORA, PAUL T, FRASER, DEBORAH ANN · 2004 to 2022
$10.0M
NIGMS NIH HHS R25 GM071638NIGMS NIH HHS UL1 GM118979
6 · The paper itself

Abstract

The identification of glycoside hydrolases (GHs) for efficient polysaccharide deconstruction is essential for the development of biofuels. Here, we investigate the potential of sequential HMM-profile identification for the rapid and precise identification of the multi-domain architecture of GHs from various datasets. First, as a validation, we successfully reannotated >98% of the biochemically characterized enzymes listed on the CAZy database. Next, we analyzed the 43 million non-redundant sequences from the M5nr data and identified 322,068 unique GHs. Finally, we searched 129 assembled metagenomes retrieved from MG-RAST for environmental GHs and identified 160,790 additional enzymes. Although most identified sequences corresponded to single domain enzymes, many contained several domains, including known accessory domains and some domains never identified in association with GH. Several sequences displayed multiple catalytic domains and few of these potential multi-activity proteins combined potentially synergistic domains. Finally, we produced and confirmed the biochemical activities of a GH5-GH10 cellulase-xylanase and a GH11-CE4 xylanase-esterase. Globally, this "gene to enzyme pipeline" provides a rationale for mining large datasets in order to identify new catalysts combining unique properties for the efficient deconstruction of polysaccharides.

Indexed as

CatalysisCatalytic DomainCellulaseComputational BiologyDatabases, ProteinGlycoside HydrolasesMarkov ChainsMetagenomeCellulaseGlycoside Hydrolases

Identifiers

PMID31300677
PMCPMC6626019

What OpenQuestion holds

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LicenceCC BY
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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.