Evidence map›Paper›PMID 29784878›Full record

ArticleThe Journal of biological chemistry2018

Oxidative decarboxylation of pyruvate by 1-deoxy-d-xyulose 5-phosphate synthase, a central metabolic enzyme in bacteria.

Alicia A DeColli, Natalia S Nemeria, Ananya Majumdar, Gary J Gerfen, Frank Jordan, Caren L Freel Meyers

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

18 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  9. Potent Inhibition ofACS infectious diseases · 2024
    Article
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  12. Article
  13. Strategies for enhancing terpenoids accumulation in microalgae.Applied microbiology and biotechnology · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

6 authors at 4 institutions in 1 country.

Alicia A DeColliFrom the Departments of Pharmacology and Molecular Sciences and.
Natalia S Nemeriathe Department of Chemistry, Rutgers University, Newark, New Jersey 07102, and.
Ananya MajumdarChemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Gary J Gerfenthe Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461.
Frank Jordanthe Department of Chemistry, Rutgers University, Newark, New Jersey 07102, and.
Caren L Freel MeyersFrom the Departments of Pharmacology and Molecular Sciences and cmeyers@jhmi.edu.
Johns Hopkins University · USRutgers, The State University of New Jersey · USAlbert Einstein College of Medicine · USJohns Hopkins Medicine · US

Funding

PHARMACOLOGY TRAINING GRANTT32GM008763 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI FREEL MEYERS, CAREN L. · 2000 to 2019
$6.1M
Targeting Non-mammalian Isoprenoid BiosynthesisR01GM084998 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI FREEL MEYERS, CAREN L. · 2010 to 2019
$3.0M
Mechanistic Issues Related to Aging on Human 2-Oxoglutarate Dehydrogenase ComplexR15GM116077 · NIGMS · RUTGERS THE STATE UNIV OF NJ NEWARK · PI JORDAN, FRANK · 2015 to 2015
$369k
NIGMS NIH HHS R01 GM084998NIGMS NIH HHS R15 GM116077NIGMS NIH HHS T32 GM008763
6 · The paper itself

Abstract

The underexploited antibacterial target 1-deoxy-d-xyluose 5-phosphate (DXP) synthase catalyzes the thiamin diphosphate (ThDP)-dependent formation of DXP from pyruvate and d-glyceraldehyde 3-phosphate (d-GAP). DXP is an essential intermediate in the biosynthesis of ThDP, pyridoxal phosphate, and isoprenoids in many pathogenic bacteria. DXP synthase catalyzes a distinct mechanism in ThDP decarboxylative enzymology in which the first enzyme-bound pre-decarboxylation intermediate, C2α-lactyl-ThDP (LThDP), is stabilized by DXP synthase in the absence of d-GAP, and d-GAP then induces efficient LThDP decarboxylation. Despite the observed LThDP accumulation and lack of evidence for C2α-carbanion formation in the absence of d-GAP, CO

Indexed as

BacteriaCatalysisDecarboxylationOxidation-ReductionOxygenPyruvatesSubstrate SpecificityThiamine PyrophosphateTransferasesdeoxyxylulose-5-phosphate synthaseOxygenPyruvatesThiamine PyrophosphateTransferasesdecarboxylaseDXP synthaseenzyme mechanismoxidation-reduction (redox)oxidative decarboxylationoxygenaseoxygen bindingpyridoxal phosphatethiamine

Identifiers

PMID29784878
PMCPMC6052232
OpenAlexW2803933651

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.