Evidence map›Paper›PMID 21421758›Full record

ArticleJournal of bacteriology2011

Role of maltose enzymes in glycogen synthesis by Escherichia coli.

Jong-Tae Park, Jae-Hoon Shim, Phuong Lan Tran, In-Hee Hong, Hwan-Ung Yong, Ershita Fitria Oktavina, Hai Dang Nguyen, Jung-Wan Kim, Tae Soo Lee, Sung-Hoon Park and 2 more

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.0field-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

31 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Production of Large-Ring Cyclodextrins by Amylomaltases.Molecules (Basel, Switzerland) · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  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

12 authors at 6 institutions in 3 countries.

Jong-Tae ParkCenter for Agricultural Biomaterials and Department of Food Science and Biotechnology, Seoul National University, Seoul 151-921, Republic of Korea.
Jae-Hoon Shim
Phuong Lan Tran
In-Hee Hong
Hwan-Ung Yong
Ershita Fitria Oktavina
Hai Dang Nguyen
Jung-Wan Kim
Tae Soo Lee
Sung-Hoon Park
Winfried Boos
Kwan-Hwa Park
Incheon National University · KRSeoul National University · KRAgriculture and Agri-Food Canada · CAChungnam National University · KRHallym University · KRUniversity of Konstanz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutants with deletion mutations in the glg and mal gene clusters of Escherichia coli MC4100 were used to gain insight into glycogen and maltodextrin metabolism. Glycogen content, molecular mass, and branch chain distribution were analyzed in the wild type and in ΔmalP (encoding maltodextrin phosphorylase), ΔmalQ (encoding amylomaltase), ΔglgA (encoding glycogen synthase), and ΔglgA ΔmalP derivatives. The wild type showed increasing amounts of glycogen when grown on glucose, maltose, or maltodextrin. When strains were grown on maltose, the glycogen content was 20 times higher in the ΔmalP strain (0.97 mg/mg protein) than in the wild type (0.05 mg/mg protein). When strains were grown on glucose, the ΔmalP strain and the wild type had similar glycogen contents (0.04 mg/mg and 0.03 mg/mg protein, respectively). The ΔmalQ mutant did not grow on maltose but showed wild-type amounts of glycogen when grown on glucose, demonstrating the exclusive function of GlgA for glycogen synthesis in the absence of maltose metabolism. No glycogen was found in the ΔglgA and ΔglgA ΔmalP strains grown on glucose, but substantial amounts (0.18 and 1.0 mg/mg protein, respectively) were found when they were grown on maltodextrin. This demonstrates that the action of MalQ on maltose or maltodextrin can lead to the formation of glycogen and that MalP controls (inhibits) this pathway. In vitro, MalQ in the presence of GlgB (a branching enzyme) was able to form glycogen from maltose or linear maltodextrins. We propose a model of maltodextrin utilization for the formation of glycogen in the absence of glycogen synthase.

Indexed as

Escherichia coliEscherichia coli ProteinsGene DeletionGlucoseGlucosyltransferasesGlycogenGlycogen Debranching Enzyme SystemGlycogen SynthaseMaltosePolysaccharides4 alpha-glucanotransferaseEscherichia coli ProteinsGlucoseGlucosyltransferasesGlycogenGlycogen Debranching Enzyme SystemGlycogen Synthasemaltodextrinmaltodextrin phosphorylaseMaltosePolysaccharides

Identifiers

PMID21421758
PMCPMC3133173
OpenAlexW2038528328

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.