Evidence map›Paper›PMID 16672483›Full record

ArticleApplied and environmental microbiology2006

Genomic and proteomic analyses of the agarolytic system expressed by Saccharophagus degradans 2-40.

Nathan A Ekborg, Larry E Taylor, Atkinson G Longmire, Bernard Henrissat, Ronald M Weiner, Steven W Hutcheson

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.3field-weighted citation impact, top 10% 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

42 citing papers in PubMed, 118 citations in OpenAlex.

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  7. The structure of PfGH50B, an agarase from the marine bacterium Pseudoalteromonas fuliginea PS47.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  8. Dual Agarolytic Pathways in a Marine Bacterium,Applied and environmental microbiology · 2020
    Article
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  12. Review
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  15. Genomic diversification of giant enteric symbionts reflects host dietary lifestyles.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Review
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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

6 authors at 2 institutions in 2 countries.

Nathan A EkborgDepartment of Cell Biology and Molecular Genetics, Microbiology Building, University of Maryland, College Park, MD 20742, USA.
Larry E Taylor
Atkinson G Longmire
Bernard Henrissat
Ronald M Weiner
Steven W Hutcheson
University of Maryland, College Park · USArchitecture et Fonction des Macromolécules Biologiques · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Saccharophagus degradans 2-40 (formerly Microbulbifer degradans 2-40) is a marine gamma-subgroup proteobacterium capable of degrading many complex polysaccharides, such as agar. While several agarolytic systems have been characterized biochemically, the genetics of agarolytic systems have been only partially determined. By use of genomic, proteomic, and genetic approaches, the components of the S. degradans 2-40 agarolytic system were identified. Five agarases were identified in the S. degradans 2-40 genome. Aga50A and Aga50D include GH50 domains. Aga86C and Aga86E contain GH86 domains, whereas Aga16B carries a GH16 domain. Novel family 6 carbohydrate binding modules (CBM6) were identified in Aga16B and Aga86E. Aga86C has an amino-terminal acylation site, suggesting that it is surface associated. Aga16B, Aga86C, and Aga86E were detected by mass spectrometry in agarolytic fractions obtained from culture filtrates of agar-grown cells. Deletion analysis revealed that aga50A and aga86E were essential for the metabolism of agarose. Aga16B was shown to endolytically degrade agarose to release neoagarotetraose, similarly to a beta-agarase I, whereas Aga86E was demonstrated to exolytically degrade agarose to form neoagarobiose. The agarolytic system of S. degradans 2-40 is thus predicted to be composed of a secreted endo-acting GH16-dependent depolymerase, a surface-associated GH50-dependent depolymerase, an exo-acting GH86-dependent agarase, and an alpha-neoagarobiose hydrolase to release galactose from agarose.

Indexed as

Genome, BacterialProteomeAlteromonadaceaeBacterial ProteinsEscherichia coliGene DeletionGlycoside HydrolasesMolecular Sequence DataPhylogenySequence Analysis, DNAagaraseBacterial ProteinsGlycoside HydrolasesProteome

Identifiers

PMID16672483
PMCPMC1472325
OpenAlexW1969705632

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.