Evidence map›Paper›PMID 27872187›Full record

ArticleThe Journal of biological chemistry2017

Galactomannan Catabolism Conferred by a Polysaccharide Utilization Locus of Bacteroides ovatus: ENZYME SYNERGY AND CRYSTAL STRUCTURE OF A β-MANNANASE.

Viktoria Bågenholm, Sumitha K Reddy, Hanene Bouraoui, Johan Morrill, Evelina Kulcinskaja, Constance M Bahr, Oskar Aurelius, Theresa Rogers, Yao Xiao, Derek T Logan and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
19.9field-weighted citation impact, top 1% 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

60 citing papers in PubMed, 114 citations in OpenAlex.

  1. Review
  2. Applied and environmental microbiology · 2026
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  8. Article
  9. Article
  10. Genetic analysis of a β-1,3/1,4-glucan utilization gene cluster inBioscience of microbiota, food and health · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. The catabolic specialization of the marine bacteriumApplied and environmental microbiology · 2024
    Article
  15. Inducible CRISPR-targeted "knockdown" of human gutProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Review
  17. Article
  18. Article
  19. Potential of Wood Hemicelluloses and Their Derivates as Food Ingredients.Journal of agricultural and food chemistry · 2023
    Review
  20. 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

13 authors at 2 institutions in 2 countries.

Viktoria BågenholmFrom the Department of Biochemistry and Structural Biology, Lund University P. O. Box 124, S-221 00 Lund, Sweden and.
Sumitha K ReddyFrom the Department of Biochemistry and Structural Biology, Lund University P. O. Box 124, S-221 00 Lund, Sweden and.
Hanene BouraouiFrom the Department of Biochemistry and Structural Biology, Lund University P. O. Box 124, S-221 00 Lund, Sweden and.
Johan MorrillFrom the Department of Biochemistry and Structural Biology, Lund University P. O. Box 124, S-221 00 Lund, Sweden and.
Evelina KulcinskajaFrom the Department of Biochemistry and Structural Biology, Lund University P. O. Box 124, S-221 00 Lund, Sweden and.
Constance M Bahrthe Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48109.
Oskar AureliusFrom the Department of Biochemistry and Structural Biology, Lund University P. O. Box 124, S-221 00 Lund, Sweden and.
Theresa Rogersthe Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48109.
Yao Xiaothe Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48109.
Derek T LoganFrom the Department of Biochemistry and Structural Biology, Lund University P. O. Box 124, S-221 00 Lund, Sweden and.
Eric C Martensthe Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48109.
Nicole M Koropatkinthe Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48109.
Henrik StålbrandFrom the Department of Biochemistry and Structural Biology, Lund University P. O. Box 124, S-221 00 Lund, Sweden and henrik.stalbrand@biochemistry.lu.se.
Lund University · SEUniversity of Michigan–Ann Arbor · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A recently identified polysaccharide utilization locus (PUL) from Bacteroides ovatus ATCC 8483 is transcriptionally up-regulated during growth on galacto- and glucomannans. It encodes two glycoside hydrolase family 26 (GH26) β-mannanases, BoMan26A and BoMan26B, and a GH36 α-galactosidase, BoGal36A. The PUL also includes two glycan-binding proteins, confirmed by β-mannan affinity electrophoresis. When this PUL was deleted, B. ovatus was no longer able to grow on locust bean galactomannan. BoMan26A primarily formed mannobiose from mannan polysaccharides. BoMan26B had higher activity on galactomannan with a high degree of galactosyl substitution and was shown to be endo-acting generating a more diverse mixture of oligosaccharides, including mannobiose. Of the two β-mannanases, only BoMan26B hydrolyzed galactoglucomannan. A crystal structure of BoMan26A revealed a similar structure to the exo-mannobiohydrolase CjMan26C from Cellvibrio japonicus, with a conserved glycone region (-1 and -2 subsites), including a conserved loop closing the active site beyond subsite -2. Analysis of cellular location by immunolabeling and fluorescence microscopy suggests that BoMan26B is surface-exposed and associated with the outer membrane, although BoMan26A and BoGal36A are likely periplasmic. In light of the cellular location and the biochemical properties of the two characterized β-mannanases, we propose a scheme of sequential action by the glycoside hydrolases encoded by the β-mannan PUL and involved in the β-mannan utilization pathway in B. ovatus. The outer membrane-associated BoMan26B initially acts on the polysaccharide galactomannan, producing comparably large oligosaccharide fragments. Galactomanno-oligosaccharides are further processed in the periplasm, degalactosylated by BoGal36A, and subsequently hydrolyzed into mainly mannobiose by the β-mannanase BoMan26A.

Indexed as

Bacteroidesbeta-MannosidaseCatalysisCrystallography, X-RayGalactoseHydrolysisMannansPolysaccharidesProtein ConformationSubstrate Specificitybeta-MannosidasegalactomannanGalactoseMannansPolysaccharidesBacteroides ovatuscarbohydrate metabolismenzyme kineticsgalactomannanglycobiologyglycoside hydrolaseGram-negative bacteriahuman gut bacteriapolysaccharide utilization locistructure-function

Identifiers

PMID27872187
PMCPMC5217682
OpenAlexW2554408808

What OpenQuestion holds

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Registered trials

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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.