Evidence map›Paper›PMID 2646272›Full record

ArticleJournal of bacteriology1989

A single point mutation results in a constitutively activated and feedback-resistant chorismate mutase of Saccharomyces cerevisiae.

T Schmidheini, P Sperisen, G Paravicini, R Hütter, G Braus

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. A flexible, allosteric loop regulates protein activity and rewires electrostatics.Protein science : a publication of the Protein Society · 2025
    Article
  3. Mixed, nonclassical behavior in a classic allosteric protein.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Review
  5. Biosynthesis of tetrahydropapaverine and semisynthesis of papaverine in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Coevolution of transcriptional and allosteric regulation at the chorismate metabolic branch point of Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  13. Article
  14. Separation of inhibition and activation of the allosteric yeast chorismate mutase.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  15. A glutamate residue in the catalytic center of the yeast chorismate mutase restricts enzyme activity to acidic conditions.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  16. Article
  17. Article
  18. In vivo catalysis of a metabolically essential reaction by an antibody.Proceedings of the National Academy of Sciences of the United States of America · 1991
    Article
  19. Review
  20. 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

5 authors at 1 institution in 1 country.

T SchmidheiniInstitute of Microbiology, Swiss Federal Institute of Technology, Zurich.
P Sperisen
G Paravicini
R Hütter
G Braus
École Polytechnique Fédérale de Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Saccharomyces cerevisiae ARO7 gene product chorismate mutase, a single-branch-point enzyme in the aromatic amino acid biosynthetic pathway, is activated by tryptophan and subject to feedback inhibition by tyrosine. The ARO7 gene was cloned on a 2.05-kilobase EcoRI fragment. Northern (RNA) analysis revealed a 0.95-kilobase poly(A)+ RNA, and DNA sequencing determined a 771-base-pair open reading frame capable of encoding a protein 256 amino acids. In addition, three mutant alleles of ARO7 were cloned and sequenced. These encoded chorismate mutases which were unresponsive to tyrosine and tryptophan and were locked in the on state, exhibiting a 10-fold-increased basal enzyme activity. A single base pair exchange resulting in a threonine-to-isoleucine amino acid substitution in the C-terminal part of the chorismate mutase was found in all mutant strains. In contrast to other enzymes in this pathway, no significant homology between the monofunctional yeast chorismate mutase and the corresponding domains of the two bifunctional Escherichia coli enzymes was found.

Indexed as

GenesGenes, FungalMutationAllelesAmino Acid SequenceBase SequenceChorismate MutaseCloning, MolecularFeedbackGenotypeIsomerasesKineticsMolecular Sequence DataPlasmidsRestriction MappingSaccharomyces cerevisiaeChorismate MutaseIsomerasesTyrosine

Identifiers

PMID2646272
PMCPMC209737
OpenAlexW1520921680

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.