Evidence map›Paper›PMID 9501182›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Separation of inhibition and activation of the allosteric yeast chorismate mutase.

G Schnappauf, W N Lipscomb, G H Braus

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.2field-weighted citation impact, top 49% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. A flexible, allosteric loop regulates protein activity and rewires electrostatics.Protein science : a publication of the Protein Society · 2025
    Article
  2. Article
  3. Mixed, nonclassical behavior in a classic allosteric protein.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

3 authors at 2 institutions in 2 countries.

G SchnappaufInstitut für Mikrobiologie und Genetik, Georg-August-Universität, Grisebachstrasse 8, D-37077 Göttingen, Germany.
W N Lipscomb
G H Braus
University of Göttingen · DEHarvard University · US

Funding

STRUCTURE/FUNCTION OF BIOLOGICALLY ACTIVE MOLECULESR01GM006920 · NIGMS · HARVARD UNIVERSITY · PI LIPSCOMB, WILLIAM N · 1985 to 2003
$1.2M
STRUCTURE/FUNCTION OF BIOLOGICALLY ACTIVE MOLECULESR37GM006920 · NIGMS · HARVARD UNIVERSITY · PI LIPSCOMB, WILLIAM N · 1986 to 1995
–
NIGMS NIH HHS GM06920NIGMS NIH HHS R01 GM006920
6 · The paper itself

Abstract

Yeast chorismate mutase (EC 5.4.99.5) shows homotropic activation by the substrate, allosteric activation by tryptophan, and allosteric inhibition by tyrosine. In this study mutants of chorismate mutase have been found that remain sensitive to one allosteric effector (tryptophan) but insensitive to the other (tyrosine). These mutations are located in the catalytic domain: loop 220s (212-226) and helix 12 (227-251). The first example starts with the Thr-266 --> Ile mutant that had previously been shown to be locked in the activated R state. The additional mutation Ile-225 --> Thr unlocks the R state and restores the activation by tryptophan but not the inhibition by tyrosine. The second example refers to a molecular trigger for the switch between the T and R state: a hydrogen-bonded system, which stabilizes only the T state, from Tyr-234 to Glu-23 to Arg-157. Various mutants of Tyr-234, especially Tyr-234 --> Phe, are unresponsive to tyrosine but are activated by tryptophan. This separation of activation from inhibition may indicate a pathway for activation that is independent of the allosteric transition and may also be consistent with an intermediate structure between T and R states.

Indexed as

Allosteric RegulationAllosteric SiteChorismate MutaseEnzyme ActivationModels, BiologicalModels, MolecularMutationProtein Structure, SecondarySaccharomyces cerevisiaeTryptophanTyrosineChorismate MutaseTryptophanTyrosine

Identifiers

PMID9501182
PMCPMC19661
OpenAlexW2005316000

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.