Evidence map›Paper›PMID 7563125›Full record

ArticleJournal of molecular evolution1995

Primary structure and eubacterial relationships of the pyruvate:ferredoxin oxidoreductase of the amitochondriate eukaryote Trichomonas vaginalis.

I Hrdý, M Müller

Abstract readComparative Study
PubMed
In one paragraph

Article in Journal of molecular evolution, 1995. 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
4.5field-weighted citation impact, top 5% 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, 112 citations in OpenAlex.

  1. Article
  2. Article
  3. N-Terminal Segment ofBiomolecules · 2020
    Article
  4. Article
  5. Article
  6. Article
  7. Biochemistry and evolution of anaerobic energy metabolism in eukaryotes.Microbiology and molecular biology reviews : MMBR · 2012
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Lipoic acid metabolism in microbial pathogens.Microbiology and molecular biology reviews : MMBR · 2010
    Review
  13. Diversity and reductive evolution of mitochondria among microbial eukaryotes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2010
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Multiple secondary origins of the anaerobic lifestyle in eukaryotes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2006
    Review
  19. Article
  20. Origin and evolution of the mitochondrial proteome.Microbiology and molecular biology reviews : MMBR · 2000
    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.

I HrdýRockefeller University, New York, NY 10021, USA.
M Müller
Rockefeller University · US

Funding

BIOCHEMICAL CYTOLOGY OF TRICHOMONAS VAGINALISR01AI011942 · NIAID · ROCKEFELLER UNIVERSITY · PI MULLER, MIKLOS · 1985 to 2003
$1.3M
AMINO ACID ANALYZERS15CA046157 · NCI · ROCKEFELLER UNIVERSITY · PI LEDERBERG, JOSHUA · 1987 to 1987
–
NCI NIH HHS CA 46157NIAID NIH HHS AI 11942
6 · The paper itself

Abstract

In the eukaryotic unicellular organism Trichomonas vaginalis a key step of energy metabolism, the oxidative decarboxylation of pyruvate with the formation of acetyl-CoA, is catalyzed by the iron-sulfur protein pyruvate:ferredoxin oxidoreductase (PFO) and not by the almost-ubiquitous pyruvate dehydrogenase multienzyme complex. This enzyme is localized in the hydrogenosome, an organelle bounded by a double membrane. PFO and its closely related homolog, pyruvate:flavodoxin oxidoreductase, are enzymes found in a number of archaebacteria and eubacteria. The presence of these enzymes in eukaryotes is restricted, however, to a few amitochondriate groups. To gain more insight into the evolutionary relationships of T. vaginalis PFO we determined the primary structure of its two genes (pfoA and pfoB). The deduced amino acid sequences showed 95% positional identity. Motifs implicated in related enzymes in liganding the Fe-S centers and thiamine pyrophosphate were well conserved. The T. vaginalis PFOs were found to be homologous to eubacterial pyruvate:flavodoxin oxidoreductases and showed about 40% amino acid identity to these enzymes over their entire length. Lack of eubacterial PFO sequences precluded a comparison. pfoA and pfoB revealed a greater distance from related enzymes of Archaebacteria. The conceptual translation of the nucleotide sequences predicted an amino-terminal pentapeptide not present in the mature protein. This processed leader sequence was similar to but shorter than leader sequences noted in other hydrogenosomal proteins.(ABSTRACT TRUNCATED AT 250 WORDS)

Indexed as

PhylogenyAmino Acid SequenceAnimalsBacteriaBacterial ProteinsBase SequenceElectron TransportEnergy MetabolismEukaryotic CellsFermentationGenes, BacterialGenes, ProtozoanKetone OxidoreductasesMolecular Sequence DataOpen Reading FramesProtein Sorting SignalsBacterial ProteinsKetone OxidoreductasesProtein Sorting SignalsProtozoan Proteinspyruvate-flavodoxin oxidoreductasePyruvate Synthase

Identifiers

PMID7563125
OpenAlexW1485008430

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.