Evidence map›Paper›PMID 24014032›Full record

ArticleThe Journal of biological chemistry2013

The thiamine biosynthetic enzyme ThiC catalyzes multiple turnovers and is inhibited by S-adenosylmethionine (AdoMet) metabolites.

Lauren D Palmer, Diana M Downs

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

30 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. On the Evolutionary History of the Twenty Encoded Amino Acids.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022
    Review
  8. Article
  9. Natural Variation in Vitamin BFrontiers in plant science · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. TheFrontiers in plant science · 2021
    Article
  14. Microbial Cell Factories for Green Production of Vitamins.Frontiers in bioengineering and biotechnology · 2021
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. 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

2 authors at 1 institution in 1 country.

Lauren D PalmerFrom the Department of Microbiology, University of Georgia, Athens, Georgia 30602.
Diana M DownsFrom the Department of Microbiology, University of Georgia, Athens, Georgia 30602. Electronic address: dmdowns@uga.edu.
University of Georgia · US

Funding

NOVEL SYNTHETIC PATHWAY FOR THE PYRIMIDINE OF THIAMINER01GM047296 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DOWNS, DIANA M. · 1993 to 2010
$3.1M
NIGMS NIH HHS GM47296NIGMS NIH HHS R01 GM047296
6 · The paper itself

Abstract

ThiC (4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase; EC 4.1.99.17) is a radical S-adenosylmethionine (AdoMet) enzyme that uses a [4Fe-4S](+) cluster to reductively cleave AdoMet to methionine and a 5'-deoxyadenosyl radical that initiates catalysis. In plants and bacteria, ThiC converts the purine intermediate 5-aminoimidazole ribotide to 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate, an intermediate of thiamine pyrophosphate (coenzyme B1) biosynthesis. In this study, assay conditions were implemented that consistently generated 5-fold molar excess of HMP, demonstrating that ThiC undergoes multiple turnovers. ThiC activity was improved by in situ removal of product 5'-deoxyadenosine. The activity was inhibited by AdoMet metabolites S-adenosylhomocysteine, adenosine, 5'-deoxyadenosine, S-methyl-5'-thioadenosine, methionine, and homocysteine. Neither adenosine nor S-methyl-5'-thioadenosine had been shown to inhibit radical AdoMet enzymes, suggesting that ThiC is distinct from other family members. The parameters for improved ThiC activity and turnover described here will facilitate kinetic and mechanistic analyses of ThiC.

Indexed as

Bacterial ProteinsCatalysisKineticsS-AdenosylmethionineThiamine PyrophosphateTreponema denticolaBacterial ProteinsS-AdenosylmethionineThiamine PyrophosphateThiC protein, BacteriaEnzyme InhibitorsIron-Sulfur ProteinRadicalsS-adenosylmethionine (AdoMet)ThiamineThiamine Biosynthesis

Identifiers

PMID24014032
PMCPMC3798539
OpenAlexW2036427629

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.