Evidence map›Paper›PMID 26167158›Full record

ArticleFrontiers in microbiology2015

The primary pathway for lactate oxidation in Desulfovibrio vulgaris.

Nicolas Vita, Odile Valette, Gaël Brasseur, Sabrina Lignon, Yann Denis, Mireille Ansaldi, Alain Dolla, Laetitia Pieulle

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

21 citing papers in PubMed, 60 citations in OpenAlex.

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  16. Proteomic and Isotopic Response ofFrontiers in microbiology · 2019
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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

8 authors at 2 institutions in 1 country.

Nicolas VitaCNRS, LCB-UMR7283, Aix-Marseille Université Marseille, France.
Odile ValetteCNRS, LCB-UMR7283, Aix-Marseille Université Marseille, France.
Gaël BrasseurCNRS, LCB-UMR7283, Aix-Marseille Université Marseille, France.
Sabrina LignonCNRS, IMM-FR3479, Plate-forme Protéomique-IBISA Marseille-Protéomique Marseille, France.
Yann DenisIMM-FR3479, Plate-forme Transcriptomique Marseille, France.
Mireille AnsaldiCNRS, LCB-UMR7283, Aix-Marseille Université Marseille, France.
Alain DollaCNRS, LCB-UMR7283, Aix-Marseille Université Marseille, France.
Laetitia PieulleCNRS, LCB-UMR7283, Aix-Marseille Université Marseille, France ; Laboratoire de Chimie Bactérienne, Institut de Microbiologie de la Méditerranée, Aix-Marseille Université Marseille, France.
Laboratoire de Chimie Bactérienne · FRInstitut de Microbiologie de la Méditerranée · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ability to respire sulfate linked to lactate oxidation is a key metabolic signature of the Desulfovibrio genus. Lactate oxidation by these incomplete oxidizers generates reductants through lactate dehydrogenase (LDH) and pyruvate-ferredoxin oxidoreductase (PFOR), with the latter catalyzing pyruvate conversion into acetyl-CoA. Acetyl-CoA is the source of substrate-level phosphorylation through the production of ATP. Here, we show that these crucial steps are performed by enzymes encoded by a nonacistronic transcriptional unit named now as operon luo (for lactate utilization operon). Using a combination of genetic and biochemical techniques, we assigned a physiological role to the operon genes DVU3027-28 and DVU3032-33. The growth of mutant Δ26-28 was highly disrupted on D-lactate, whereas the growth of mutant Δ32-33 was slower on L-lactate, which could be related to a decrease in the activity of D-lactate or L-lactate oxidase in the corresponding mutants. The DVU3027-28 and DVU3032-33 genes thus encode functional D-LDH and L-LDH enzymes, respectively. Scanning of the genome for lactate utilization revealed several lactate permease and dehydrogenase homologs. However, transcriptional compensation was not observed in any of the mutants except for lactate permease. Although there is a high degree of redundancy for lactate oxidase, it is not functionally efficient in LDH mutants. This result could be related to the identification of several operon enzymes, including LDHs, in the PFOR activity bands, suggesting the occurrence of a lactate-oxidizing supermolecular structure that can optimize the performance of lactate utilization in Desulfovibrio species.

Indexed as

anaerobic lactate oxidationDesulfovibriolactate dehydrogenasepyruvate-ferredoxin oxidoreductasesulfate-reducing bacteria

Identifiers

PMID26167158
PMCPMC4481167
OpenAlexW1877605061

What OpenQuestion holds

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LicenceCC BY
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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.