Evidence map›Paper›PMID 32583284›Full record

ReviewJournal of microbiology (Seoul, Korea)2020

Phosphate sugar isomerases and their potential for rare sugar bioconversion.

Soo-Jung Kim, Yeong-Su Kim, Soo-Jin Yeom

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of microbiology (Seoul, Korea), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Taxonomic Identification of the Arctic StrainInternational journal of molecular sciences · 2023
    Article
  5. Article
  6. Article
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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 1 country.

Soo-Jung KimDepartment of Integrative Food, Bioscience and Biotechnology, Chonnam National University, Gwangju, 61186, Republic of Korea.
Yeong-Su KimWild Plants Industrialization Research Division, Baekdudaegan National Arboretum, Bonghwa, 36209, Republic of Korea. yskim@kiam.or.kr.
Soo-Jin YeomSchool of Biological Sciences and Technology, Chonnam National University, Gwangju, 61186, Republic of Korea. soojin258@jnu.ac.
Chonnam National University · KRKorea Forest Service · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphate sugar isomerases, catalyzing the isomerization between ketopentose/ketohexose phosphate and aldopentose/aldohexose phosphate, play an important role in microbial sugar metabolism. They are present in a wide range of microorganisms. They have attracted increasing research interest because of their broad substrate specificity and great potential in the enzymatic production of various rare sugars. Here, the enzymatic properties of various phosphate sugar isomerases are reviewed in terms of their substrate specificities and their applications in the production of valuable rare sugars because of their functions such as low-calorie sweeteners, bulking agents, and pharmaceutical precursor. Specifically, we focused on the industrial applications of D-ribose-5-phosphate isomerase and D-mannose-6-phosphate isomerase to produce D-allose and L-ribose, respectively.

Indexed as

Aldose-Ketose IsomerasesBacteriaGlucoseHexosesMannose-6-Phosphate IsomerasePentosesRiboseSubstrate SpecificitySweetening AgentsAldose-Ketose IsomerasesalloseGlucoseHexosesMannose-6-Phosphate IsomerasePentosesRiboseribosephosphate isomeraseSweetening Agentsbiocatalystbioconversionphosphate sugar isomeraserare sugarsubstrate specificity

Identifiers

PMID32583284
OpenAlexW3037457299

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.