Evidence map›Paper›PMID 28092359›Full record

ArticleNature chemical biology2017

Lysine relay mechanism coordinates intermediate transfer in vitamin B6 biosynthesis.

Matthew J Rodrigues, Volker Windeisen, Yang Zhang, Gabriela Guédez, Stefan Weber, Marco Strohmeier, Jeremiah W Hanes, Antoine Royant, Gwyndaf Evans, Irmgard Sinning and 3 more

Abstract read
In one paragraph

Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Guiding covalent catalysis enables a carbon-inserting rearrangement in molybdenum cofactor biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
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  4. Article
  5. Article
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  11. Structural Dynamics and Perspectives of Vitamin B6 Biosynthesis Enzymes inFrontiers in cellular and infection microbiology · 2021
    Review
  12. Article
  13. G3 (Bethesda, Md.) · 2019
    Article
  14. Review
  15. Protein structural biology using cell-free platform from wheat germ.Advanced structural and chemical imaging · 2018
    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

13 authors.

Matthew J RodriguesBiological Sciences, University of Southampton, Southampton, UK.
Volker WindeisenBiological Sciences, University of Southampton, Southampton, UK.
Yang ZhangDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.
Gabriela GuédezHeidelberg University Biochemistry Center (BZH), Heidelberg, Germany.
Stefan WeberHeidelberg University Biochemistry Center (BZH), Heidelberg, Germany.
Marco StrohmeierHeidelberg University Biochemistry Center (BZH), Heidelberg, Germany.
Jeremiah W HanesDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.
Antoine RoyantInstitut de Biologie Structurale, Université Grenoble Alpes, CNRS, CEA, Grenoble, France.
Gwyndaf EvansDiamond Light Source, Harwell Science and Innovation Campus, Didcot, UK.ORCID 0000-0002-6079-2201
Irmgard SinningHeidelberg University Biochemistry Center (BZH), Heidelberg, Germany.
Steven E EalickDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.
Tadhg P BegleyDepartment of Chemistry, Texas A&M University, College Station, Texas, USA.
Ivo TewsBiological Sciences, University of Southampton, Southampton, UK.ORCID 0000-0002-4704-1139

Funding

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
The mechanistic enzymology of thiamin biosynthesisR56DK044083 · NIDDK · TEXAS A&M UNIVERSITY · PI BEGLEY, TADHG P. · 2019 to 2019
$150k
NIDDK NIH HHS R01 DK044083NIDDK NIH HHS R37 DK044083NIDDK NIH HHS R56 DK044083
6 · The paper itself

Abstract

Substrate channeling has emerged as a common mechanism for enzymatic intermediate transfer. A conspicuous gap in knowledge concerns the use of covalent lysine imines in the transfer of carbonyl-group-containing intermediates, despite their wideuse in enzymatic catalysis. Here we show how imine chemistry operates in the transfer of covalent intermediates in pyridoxal 5'-phosphate biosynthesis by the Arabidopsis thaliana enzyme Pdx1. An initial ribose 5-phosphate lysine imine is converted to the chromophoric I

Indexed as

Arabidopsis ProteinsCarbon-Nitrogen LyasesLysineModels, MolecularMolecular StructureNitrogenous Group TransferasesVitamin B 6Arabidopsis ProteinsAt2g38230 protein, ArabidopsisCarbon-Nitrogen LyasesLysineNitrogenous Group TransferasesVitamin B 6

Identifiers

PMID28092359
PMCPMC6078385

What OpenQuestion holds

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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.