Evidence map›Paper›PMID 21162571›Full record

ArticleJournal of the American Chemical Society2011

Protein thiocarboxylate-dependent methionine biosynthesis in Wolinella succinogenes.

Kalyanaraman Krishnamoorthy, Tadhg P Begley

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-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

13 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Discovery of a novel methionine biosynthetic routeApplied and environmental microbiology · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Prokaryotic ubiquitin-like protein modification.Annual review of microbiology · 2014
    Review
  10. Article
  11. Review
  12. Article
  13. Sulfur incorporation into biomolecules: recent advances.Critical reviews in biochemistry and molecular biology
    Review
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.

Kalyanaraman KrishnamoorthyDepartment of Chemistry, Texas A&M University, College Station, Texax 77840, United States.
Tadhg P Begley
Texas A&M University · US

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 DK44083NIDDK NIH HHS R01 DK044083NIDDK NIH HHS R37 DK044083NIDDK NIH HHS R56 DK044083
6 · The paper itself

Abstract

Thiocarboxylated proteins are important intermediates in a variety of biochemical sulfide transfer reactions. Here we identify a protein thiocarboxylate-dependent methionine biosynthetic pathway in Wolinella succinogenes. In this pathway, the carboxy terminal alanine of a novel sulfur transfer protein, HcyS-Ala, is removed in a reaction catalyzed by a metalloprotease, HcyD. HcyF, an ATP-utilizing enzyme, catalyzes the adenylation of HcyS. HcyS acyl-adenylate then undergoes nucleophilic substitution by bisulfide produced by Sir to give the HcyS thiocarboxylate. This adds to O-acetylhomoserine to give HcyS-homocysteine in a PLP-dependent reaction catalyzed by MetY. HcyD-mediated hydrolysis liberates homocysteine. A final methylation completes the biosynthesis. The biosynthetic gene cluster also encodes the enzymes involved in the conversion of sulfate to sulfide suggesting that sulfate is the sulfur source for protein thiocarboxylate formation in this system.

Indexed as

AlanineBiocatalysisDipeptidesMetalloproteasesMethionineMolecular StructureSulfhydryl CompoundsWolinellaAlanineDipeptidesMetalloproteasesMethionineSulfhydryl Compounds

Identifiers

PMID21162571
PMCPMC3089676
OpenAlexW2048221966

What OpenQuestion holds

Textmetadata
LicenceTDM
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.