Evidence map›Paper›PMID 29733852›Full record

ArticleJournal of molecular biology2018

Characterizing Lysine Acetylation of Isocitrate Dehydrogenase in Escherichia coli.

Sumana Venkat, Hao Chen, Alleigh Stahman, Denver Hudson, Paige McGuire, Qinglei Gan, Chenguang Fan

Abstract read
In one paragraph

Article in Journal of molecular biology, 2018. 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
1.4field-weighted citation impact, top 20% 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, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. eLife · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Characterizing lysine acetylation of glucokinase.Protein science : a publication of the Protein Society · 2024
    Article
  12. Bacterial protein acetylation: mechanisms, functions, and methods for study.Frontiers in cellular and infection microbiology · 2024
    Review
  13. Molecular Typing ofJournal of pharmacy & bioallied sciences · 2023
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Lysine acetylation ofFrontiers in bioengineering and biotechnology · 2022
    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

7 authors at 1 institution in 1 country.

Sumana VenkatDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, United States; Cell and Molecular Biology Program, University of Arkansas, Fayetteville, AR 72701, United States.
Hao ChenDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, United States; Cell and Molecular Biology Program, University of Arkansas, Fayetteville, AR 72701, United States.
Alleigh StahmanDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, United States.
Denver HudsonDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, United States.
Paige McGuireDepartment of Biological Sciences, University of Arkansas, Fayetteville, AR 72701, United States.
Qinglei GanDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, United States.
Chenguang FanDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, United States; Cell and Molecular Biology Program, University of Arkansas, Fayetteville, AR 72701, United States. Electronic address: cf021@uark.edu.
University of Arkansas at Fayetteville · US

Funding

Expanding the genetic code in SalmonellaR21AI119813 · NIAID · YALE UNIVERSITY · PI FAN, CHENGUANG · 2015 to 2016
$424k
NIAID NIH HHS R21 AI119813
6 · The paper itself

Abstract

The Escherichia coli isocitrate dehydrogenase (ICDH) is one of the tricarboxylic acid cycle enzymes, playing key roles in energy production and carbon flux regulation. E. coli ICDH was the first bacterial enzyme shown to be regulated by reversible phosphorylation. However, the effect of lysine acetylation on E. coli ICDH, which has no sequence similarity with its counterparts in eukaryotes, is still unclear. Based on previous studies of E. coli acetylome and ICDH crystal structures, eight lysine residues were selected for mutational and kinetic analyses. They were replaced with acetyllysine by the genetic code expansion strategy or substituted with glutamine as a classic approach. Although acetylation decreased the overall ICDH activity, its effects were different site by site. Deacetylation tests demonstrated that the CobB deacetylase could deacetylate ICDH both in vivo and in vitro, but CobB was only specific for lysine residues at the protein surface. On the other hand, ICDH could be acetylated by acetyl-phosphate chemically in vitro. And in vivo acetylation tests indicated that the acetylation level of ICDH was correlated with the amounts of intracellular acetyl-phosphate. This study nicely complements previous proteomic studies to provide direct biochemical evidence for ICDH acetylation.

Indexed as

AcetylationCrystallography, X-RayEscherichia coliEscherichia coli ProteinsGenetic CodeIsocitrate DehydrogenaseKineticsLysineMutationProtein Processing, Post-TranslationalSirtuinscobB protein, E ColiEscherichia coli ProteinsIsocitrate DehydrogenaseLysineSirtuinscarbon fluxgenetic code expansionglyoxylate bypasspost-translational modificationtricarboxylic acid cycle

Identifiers

PMID29733852
PMCPMC5988991
OpenAlexW2801775705

What OpenQuestion holds

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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.