Evidence map›Paper›PMID 23077559›Full record

ArticlePloS one2012

The PduQ enzyme is an alcohol dehydrogenase used to recycle NAD+ internally within the Pdu microcompartment of Salmonella enterica.

Shouqiang Cheng, Chenguang Fan, Sharmistha Sinha, Thomas A Bobik

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

59 citing papers in PubMed, 103 citations in OpenAlex.

  1. Article
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  7. Electrochemical NAD+ regeneration in bacterial organelles.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Electrochemical cofactor recycling of bacterial microcompartments.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Electrochemical cofactor recycling of bacterial microcompartments.bioRxiv : the preprint server for biology · 2024
    Article
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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

4 authors at 3 institutions in 1 country.

Shouqiang ChengDepartment of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA.
Chenguang Fan
Sharmistha Sinha
Thomas A Bobik
Iowa State University · USNorthwestern University · USYale University · US

Funding

Dissecting the structure, function, and mechanisms of diverse protein-based metabolic organelles in bacteriaR01AI081146 · NIAID · IOWA STATE UNIVERSITY · PI BOBIK, THOMAS AQUINAS, YEATES, TODD O · 2009 to 2022
$6.5M
NIAID NIH HHS AI081146NIAID NIH HHS R01 AI081146
6 · The paper itself

Abstract

Salmonella enterica uses a bacterial microcompartment (MCP) for coenzyme B(12)-dependent 1,2-propanediol (1,2-PD) utilization (Pdu). The Pdu MCP consists of a protein shell that encapsulates enzymes and cofactors required for metabolizing 1,2-PD as a carbon and energy source. Here we show that the PduQ protein of S. enterica is an iron-dependent alcohol dehydrogenase used for 1,2-PD catabolism. PduQ is also demonstrated to be a new component of the Pdu MCP. In addition, a series of in vivo and in vitro studies show that a primary function of PduQ is to recycle NADH to NAD(+) internally within the Pdu MCP in order to supply propionaldehyde dehydrogenase (PduP) with its required cofactor (NAD(+)). Genetic tests determined that a pduQ deletion mutant grew slower than wild-type Salmonella on 1,2-PD and that this phenotype was not complemented by a non-MCP associated Adh2 from Zymomonas that catalyzes the same reaction. This suggests that PduQ has a MCP-specific function. We also found that a pduQ deletion mutant had no growth defect in a genetic background having a second mutation that prevents MCP formation which further supports a MCP-specific role for PduQ. Moreover, studies with purified Pdu MCPs demonstrated that the PduQ enzyme can convert NADH to NAD(+) to supply the PduP reaction in vitro. Cumulatively, these studies show that the PduQ enzyme is used to recycle NADH to NAD(+) internally within the Pdu MCP. To our knowledge, this is the first report of internal recycling as a mechanism for cofactor homeostasis within a bacterial MCP.

Indexed as

Alcohol DehydrogenaseAmino Acid SequenceGene DeletionHistidineMolecular Sequence DataNADOligopeptidesPropylene GlycolSalmonella entericaTransduction, GeneticAlcohol DehydrogenaseHis-His-His-His-His-HisHistidineNADOligopeptidesPropylene Glycol

Identifiers

PMID23077559
PMCPMC3471927
OpenAlexW2001792383

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.