Evidence map›Paper›PMID 11528003›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2001

Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase.

K Helmstaedt, S Krappmann, G H Braus

Abstract readComparative StudyReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.7field-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

24 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Stress Response in Bifidobacteria.Microbiology and molecular biology reviews : MMBR · 2022
    Review
  4. Article
  5. Article
  6. Engineering Allostery into Proteins.Advances in experimental medicine and biology · 2019
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Hierarchical organization of eglin c native state dynamics is shaped by competing direct and water-mediated interactions.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  17. Article
  18. Evolution of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase-encoding genes in the yeast Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  19. Article
  20. New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels.Proceedings of the National Academy of Sciences of the United States of America · 2004
    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

3 authors at 1 institution in 1 country.

K HelmstaedtAbteilung Molekulare Mikrobiologie, Institut für Mikrobiologie und Genetik, Georg-August-Universität, Grisebachstr. 8, D-37077 Göttingen, Germany.
S Krappmann
G H Braus
University of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Allosteric regulation of key metabolic enzymes is a fascinating field to study the structure-function relationship of induced conformational changes of proteins. In this review we compare the principles of allosteric transitions of the complex classical model aspartate transcarbamoylase (ATCase) from Escherichia coli, consisting of 12 polypeptides, and the less complicated chorismate mutase derived from baker's yeast, which functions as a homodimer. Chorismate mutase presumably represents the minimal oligomerization state of a cooperative enzyme which still can be either activated or inhibited by different heterotropic effectors. Detailed knowledge of the number of possible quaternary states and a description of molecular triggers for conformational changes of model enzymes such as ATCase and chorismate mutase shed more and more light on allostery as an important regulatory mechanism of any living cell. The comparison of wild-type and engineered mutant enzymes reveals that current textbook models for regulation do not cover the entire picture needed to describe the function of these enzymes in detail.

Indexed as

Allosteric RegulationAspartate CarbamoyltransferaseBinding SitesChorismate MutaseEscherichia coliModels, MolecularProtein Structure, QuaternaryProtein Structure, TertiarySignal TransductionStructure-Activity RelationshipYeastsAspartate CarbamoyltransferaseChorismate Mutase

Identifiers

PMID11528003
PMCPMC99034
OpenAlexW2114093543

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.