Evidence map›Paper›PMID 31342153›Full record

ArticleProtoplasma2019

Functional characterization of aminotransferase involved in serine and aspartate metabolism in a halotolerant cyanobacterium, Aphanothece halophytica.

Daichi Hasegawa, Kunihide Kito, Takumi Maeda, Vandna Rai, Suriyan Cha-Um, Yoshito Tanaka, Minoru Fukaya, Teruhiro Takabe

Abstract read
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In one paragraph

Article in Protoplasma, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 21% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Transcriptomic Response ofInternational journal of molecular sciences · 2024
    Article
  3. Article
  4. Review
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

8 authors at 3 institutions in 3 countries.

Daichi HasegawaGraduate School of Environmental and Human Sciences, Meijo University, Nagoya, 468-8502, Japan.
Kunihide KitoResearch Institute, Meijo University, Nagoya, 468-8502, Japan.
Takumi MaedaGraduate School of Environmental and Human Sciences, Meijo University, Nagoya, 468-8502, Japan.
Vandna RaiNational Research Center on Plant Biotechnology, Pusa Campus, New Delhi, 110012, India.
Suriyan Cha-UmNational Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency (NSTDA), Pathum Thani, 12120, Thailand.
Yoshito TanakaGraduate School of Environmental and Human Sciences, Meijo University, Nagoya, 468-8502, Japan.
Minoru FukayaFaculty of Science & Technology, Meijo University, Nagoya, 468-8502, Japan.
Teruhiro TakabeResearch Institute, Meijo University, Nagoya, 468-8502, Japan. takabe@meijo-u.ac.jp.
Meijo University · JPNational Research Centre on Plant Biotechnology · INNational Science and Technology Development Agency · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aminotransferases catalyze the reversible pyridoxal phosphate-dependent transfer of amino groups from amino acids to oxo acids and play important roles for the balance between carbon and nitrogen metabolism. In this report, four aminotransferases (Ap1-Ap4) from a halotolerant cyanobacterium Aphanothece halophytica were examined. The results revealed that Ap1 and Ap2 exhibited the aspartate:2-oxoglutarate aminotransferase (AspAT) activity whereas Ap2 catalyzed further aminotransferase activities with alanine (AlaAT) and LL-diaminopimelate (an intermediate for the synthesis of Lys/peptidoglycan) as amino donors. Ap4 exhibited bifunctional aminotransferase with phosphoserine (PSAT) and glycine (GGAT) as amino donors. No activity was observed for Ap3. We identified third gene encoding phosphoserine phosphatase (PSP) in phosphorylate serine biosynthetic pathway. The levels of mRNA for Ap2 and ApMurE encoding UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-2,6-diaminopimelate ligase were increased after salt stress. These results suggest the link among photorespiratory metabolite (serine, glycine, glyoxylate), phosphorylate serine biosynthetic pathway and aspartate metabolism via aminotransferases for the synthesis of peptidoglycan and betaine under salt stress conditions.

Indexed as

Aspartic AcidCyanobacteriaSerineTransaminasesAspartic AcidSerineTransaminasesAspartate aminotransferaseBetaineLL-diaminopimelate aminotransferasePeptidoglycanPhosphoserine aminotransferaseSalt stress

Identifiers

PMID31342153
OpenAlexW2963402513

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.