Evidence map›Paper›PMID 17309261›Full record

ArticleJournal of the American Chemical Society2007

Biosynthesis of thiamin thiazole in eukaryotes: conversion of NAD to an advanced intermediate.

Abhishek Chatterjee, Christopher T Jurgenson, Frank C Schroeder, Steven E Ealick, Tadhg P Begley

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.7field-weighted citation impact, top 6% 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

38 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. Comparative Proteomic Analysis ofJournal of fungi (Basel, Switzerland) · 2025
    Article
  4. Review
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  6. The involvement of effector memory CD4Frontiers in aging neuroscience · 2024
    Article
  7. Review
  8. Oxidative Dearomatization of PLP in Thiamin Pyrimidine Biosynthesis inJournal of the American Chemical Society · 2023
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

5 authors at 1 institution in 1 country.

Abhishek ChatterjeeDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA.
Christopher T Jurgenson
Frank C Schroeder
Steven E Ealick
Tadhg P Begley
Cornell University · US

Funding

Structural Studies of Enzymes of Thiamin BiosynthesisR01DK067081 · NIDDK · CORNELL UNIVERSITY ITHACA · PI EALICK, STEVEN E · 2005 to 2017
$4.2M
The mechanistic enzymology of thiamin biosynthesisR37DK044083 · NIDDK · TEXAS A&M UNIVERSITY · PI BEGLEY, TADHG P. · 2008 to 2017
$3.7M
The mechanistic enzymology of thiamin biosynthesisR01DK044083 · NIDDK · CORNELL UNIVERSITY ITHACA · PI BEGLEY, TADHG P. · 1991 to 2007
$2.5M
NIDDK NIH HHS DK44083NIDDK NIH HHS DK67081NIDDK NIH HHS R01 DK044083NIDDK NIH HHS R01 DK067081NIDDK NIH HHS R37 DK044083
6 · The paper itself

Abstract

Thiazole synthase catalyzes the formation of the thiazole moiety of thiamin pyrophosphate. The enzyme from Saccharomyces cerevisiae (THI4) copurifies with a set of strongly bound adenylated metabolites. One of them has been characterized as the ADP adduct of 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid. Attempts toward yielding active wild-type THI4 by releasing protein-bound metabolites have failed so far. Here, we describe the identification and characterization of two partially active mutants (C204A and H200N) of THI4. Both mutants catalyzed the release of the nicotinamide moiety from NAD to produce ADP-ribose, which was further converted to ADP-ribulose. In the presence of glycine, both the mutants catalyzed the formation of an advanced intermediate. The intermediate was trapped with ortho-phenylenediamine, yielding a stable quinoxaline derivative, which was characterized by NMR spectroscopy and ESI-MS. These observations confirm NAD as the substrate for THI4 and elucidate the early steps of this unique biosynthesis of the thiazole moiety of thiamin in eukaryotes.

Indexed as

Adenosine DiphosphateAdenosine Diphosphate RiboseEukaryotic CellsNADSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityThiamineThiamine PyrophosphateThiazolesAdenosine DiphosphateAdenosine Diphosphate RiboseNADSaccharomyces cerevisiae ProteinsTHI4 protein, S cerevisiaeThiamineThiamine PyrophosphateThiazoles

Identifiers

PMID17309261
PMCPMC2536526
OpenAlexW2071404497

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.