Evidence map›Paper›PMID 24628210›Full record

ArticleThe Journal of chemical physics2014

A model study of sequential enzyme reactions and electrostatic channeling.

Changsun Eun, Peter M Kekenes-Huskey, Vincent T Metzger, J Andrew McCammon

Abstract read
In one paragraph

Article in The Journal of chemical physics, 2014. 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
–field-weighted citation impact
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.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Vectorial channeling as a mechanism for translational control by functional prions and condensates.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Review
  8. Article
  9. Article
  10. Markov-State Transition Path Analysis of Electrostatic Channeling.The journal of physical chemistry. C, Nanomaterials and interfaces · 2019
    Article
  11. Article
  12. Review
  13. Article
  14. DNA Antenna Tile-Associated Deoxyribozyme Sensor with Improved Sensitivity.Chembiochem : a European journal of chemical biology · 2016
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  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

4 authors.

Changsun EunHoward Hughes Medical Institute, University of California, San Diego, La Jolla, California 92093, USA.
Peter M Kekenes-HuskeyDepartment of Pharmacology, University of California, San Diego, La Jolla, California 92093, USA.
Vincent T MetzgerDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093, USA.
J Andrew McCammonHoward Hughes Medical Institute, University of California, San Diego, La Jolla, California 92093, USA.

Funding

National Biomedical Computation Resource - Competitive Revision SupplementP41GM103426 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI AMARO, ROMMIE E · 2012 to 2019
$14.0M
Computationally designed phospholamban-SERCA for rectifying diabetic cardiomyopaF32HL114365 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KEKENES-HUSKEY, PETER MICHAEL · 2013 to 2013
$44k
Howard Hughes Medical InstituteNHLBI NIH HHS 1F32HL114365-01A1NHLBI NIH HHS F32 HL114365NIGMS NIH HHS P41 GM103426
6 · The paper itself

Abstract

We study models of two sequential enzyme-catalyzed reactions as a basic functional building block for coupled biochemical networks. We investigate the influence of enzyme distributions and long-range molecular interactions on reaction kinetics, which have been exploited in biological systems to maximize metabolic efficiency and signaling effects. Specifically, we examine how the maximal rate of product generation in a series of sequential reactions is dependent on the enzyme distribution and the electrostatic composition of its participant enzymes and substrates. We find that close proximity between enzymes does not guarantee optimal reaction rates, as the benefit of decreasing enzyme separation is countered by the volume excluded by adjacent enzymes. We further quantify the extent to which the electrostatic potential increases the efficiency of transferring substrate between enzymes, which supports the existence of electrostatic channeling in nature. Here, a major finding is that the role of attractive electrostatic interactions in confining intermediate substrates in the vicinity of the enzymes can contribute more to net reactive throughput than the directional properties of the electrostatic fields. These findings shed light on the interplay of long-range interactions and enzyme distributions in coupled enzyme-catalyzed reactions, and their influence on signaling in biological systems.

Indexed as

Models, MolecularStatic ElectricityEnzymesKineticsEnzymes

Identifiers

PMID24628210
PMCPMC3977847

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.