Evidence map›Paper›PMID 36881117›Full record

ArticleApplied microbiology and biotechnology2023

Unique alcohol dehydrogenases involved in algal sugar utilization by marine bacteria.

Stefan Brott, Ki Hyun Nam, François Thomas, Theresa Dutschei, Lukas Reisky, Maike Behrens, Hanna C Grimm, Gurvan Michel, Thomas Schweder, Uwe T Bornscheuer

Open access · hybridFull text read
In one paragraph

Article in Applied microbiology and biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

10 authors at 4 institutions in 3 countries.

Stefan BrottDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17487, Greifswald, Germany.ORCID http://orcid.org/0000-0003-2346-7706
Ki Hyun NamDepartment of Life Science, Pohang University of Science and Technology, Pohang, 37673, South Korea.ORCID http://orcid.org/0000-0003-3268-354X
François ThomasLaboratory of Integrative Biology of Marine Models (LBI2M), Station Biologique de Roscoff (SBR), Sorbonne Université, CNRS 29688, Roscoff, Bretagne, France.ORCID http://orcid.org/0000-0003-1896-0774
Theresa DutscheiDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17487, Greifswald, Germany.ORCID http://orcid.org/0000-0003-3053-9536
Lukas ReiskyDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17487, Greifswald, Germany.ORCID http://orcid.org/0000-0001-8957-4083
Maike BehrensDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17487, Greifswald, Germany.ORCID http://orcid.org/0000-0003-3757-588X
Hanna C GrimmDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17487, Greifswald, Germany.ORCID http://orcid.org/0000-0001-6352-0212
Gurvan MichelLaboratory of Integrative Biology of Marine Models (LBI2M), Station Biologique de Roscoff (SBR), Sorbonne Université, CNRS 29688, Roscoff, Bretagne, France.ORCID http://orcid.org/0000-0002-3009-6205
Thomas SchwederDepartment of Pharmaceutical Biotechnology, Institute of Pharmacy, University of Greifswald, 17487, Greifswald, Germany.ORCID http://orcid.org/0000-0002-7213-3596
Uwe T BornscheuerDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17487, Greifswald, Germany. uwe.bornscheuer@uni-greifswald.de.ORCID http://orcid.org/0000-0003-0685-2696
Universität Greifswald · DECentre National de la Recherche Scientifique · FRPohang University of Science and Technology · KRUniversitätsmedizin Greifswald · DE

Funding

Agence Nationale de la Recherche ANR-18-CE02-0001Deutsche Forschungsgemeinschaft BO 1862/17-1Deutsche Forschungsgemeinschaft BO 1862/17-2Deutsche Forschungsgemeinschaft SCHW 595/10-2
6 · The paper itself

Abstract

Marine algae produce complex polysaccharides, which can be degraded by marine heterotrophic bacteria utilizing carbohydrate-active enzymes. The red algal polysaccharide porphyran contains the methoxy sugar 6-O-methyl-D-galactose (G6Me). In the degradation of porphyran, oxidative demethylation of this monosaccharide towards D-galactose and formaldehyde occurs, which is catalyzed by a cytochrome P450 monooxygenase and its redox partners. In direct proximity to the genes encoding for the key enzymes of this oxidative demethylation, genes encoding for zinc-dependent alcohol dehydrogenases (ADHs) were identified, which seem to be conserved in porphyran utilizing marine Flavobacteriia. Considering the fact that dehydrogenases could play an auxiliary role in carbohydrate degradation, we aimed to elucidate the physiological role of these marine ADHs. Although our results reveal that the ADHs are not involved in formaldehyde detoxification, a knockout of the ADH gene causes a dramatic growth defect of Zobellia galactanivorans with G6Me as a substrate. This indicates that the ADH is required for G6Me utilization. Complete biochemical characterizations of the ADHs from Formosa agariphila KMM 3901

Indexed as

GalactoseRhodophytaCarbohydratesOxidoreductasesPolysaccharidesCarbohydratesGalactoseOxidoreductasesPolysaccharidesAlcohol dehydrogenaseAuxiliary activityBacteroidetesCAZymePorphyranZobellia galactanivorans

Identifiers

PMID36881117
PMCPMC10033563
OpenAlexW4323347533

What OpenQuestion holds

Textfull text, public
LicenceCC BY
measurements read138
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.