Evidence map›Paper›PMID 34019879›Full record

ArticleThe Journal of biological chemistry

Structures and kinetics of Thermotoga maritima MetY reveal new insights into the predominant sulfurylation enzyme of bacterial methionine biosynthesis.

Jodi L Brewster, Petr Pachl, James L O McKellar, Maria Selmer, Christopher J Squire, Wayne M Patrick

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

14 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Engineering of methionine-auxotrophMetabolic engineering communications · 2024
    Article
  8. pH-dependent regulation of an acidophilicApplied and environmental microbiology · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Sulfur incorporation into biomolecules: recent advances.Critical reviews in biochemistry and molecular biology
    Review
  14. 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 5 institutions in 3 countries.

Jodi L BrewsterDepartment of Biochemistry, University of Otago, Dunedin, New Zealand.
Petr PachlInstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Prague, Czech Republic.
James L O McKellarDepartment of Biochemistry, University of Otago, Dunedin, New Zealand.
Maria SelmerDepartment of Cell and Molecular Biology, Uppsala University, Uppsala, Sweden.
Christopher J SquireSchool of Biological Sciences, University of Auckland, Auckland, New Zealand.
Wayne M PatrickCentre for Biodiscovery, School of Biological Sciences, Victoria University of Wellington, Wellington, New Zealand. Electronic address: wayne.patrick@vuw.ac.nz.
University of Otago · NZCzech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZUniversity of Auckland · NZUppsala University · SEVictoria University of Wellington · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial methionine biosynthesis can take place by either the trans-sulfurylation route or direct sulfurylation. The enzymes responsible for trans-sulfurylation have been characterized extensively because they occur in model organisms such as Escherichia coli. However, direct sulfurylation is actually the predominant route for methionine biosynthesis across the phylogenetic tree. In this pathway, most bacteria use an O-acetylhomoserine aminocarboxypropyltransferase (MetY) to catalyze the formation of homocysteine from O-acetylhomoserine and bisulfide. Despite the widespread distribution of MetY, this pyridoxal 5'-phosphate-dependent enzyme remains comparatively understudied. To address this knowledge gap, we have characterized the MetY from Thermotoga maritima (TmMetY). At its optimal temperature of 70 °C, TmMetY has a turnover number (apparent k

Indexed as

Bacterial ProteinsBiosynthetic PathwaysCrystallography, X-RayKineticsMethionineModels, MolecularThermotoga maritimaBacterial ProteinsMethionineenzyme kineticsenzyme mechanismmethionineprotein structureX-ray crystallography

Identifiers

PMID34019879
PMCPMC8191291
OpenAlexW3162212775

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.