Evidence map›Paper›PMID 29352105›Full record

ArticleThe Journal of biological chemistry2018

An ornithine ω-aminotransferase required for growth in the absence of exogenous proline in the archaeon

Ren-Chao Zheng, Shin-Ichi Hachisuka, Hiroya Tomita, Tadayuki Imanaka, Yu-Guo Zheng, Makoto Nishiyama, Haruyuki Atomi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. 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
0.4field-weighted citation impact, top 46% 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, 11 citations in OpenAlex.

  1. SmsB-SmsC machinery inApplied and environmental microbiology · 2025
    Article
  2. Article
  3. An energy-conserving reaction in amino acid metabolism catalyzed by arginine synthetase.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. 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

7 authors at 5 institutions in 2 countries.

Ren-Chao ZhengFrom the Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan.
Shin-Ichi HachisukaFrom the Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan.
Hiroya TomitaFrom the Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan.
Tadayuki ImanakaCREST, Japan Science and Technology Agency, 7, Gobancho, Chiyoda-ku, Tokyo 102-0076, Japan.
Yu-Guo Zhengthe College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou 310032, China.
Makoto Nishiyamathe Biotechnology Research Center, University of Tokyo, 1-1-1, Yayoi, Bunkyo-ku Tokyo 113-8657, Japan, and.
Haruyuki AtomiFrom the Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan, atomi@sbchem.kyoto-u.ac.jp.
Kyoto University · JPJapan Science and Technology Agency · JPRitsumeikan University · JPThe University of Tokyo · JPZhejiang University of Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aminotransferases are pyridoxal 5'-phosphate-dependent enzymes that catalyze reversible transamination reactions between amino acids and α-keto acids, and are important for the cellular metabolism of nitrogen. Many bacterial and eukaryotic ω-aminotransferases that use l-ornithine (Orn), l-lysine (Lys), or γ-aminobutyrate (GABA) have been identified and characterized, but the corresponding enzymes from archaea are unknown. Here, we examined the activity and function of TK2101, a gene annotated as a GABA aminotransferase, from the hyperthermophilic archaeon

Indexed as

Amino Acid SequenceArchaeal ProteinsConserved SequenceGene Knockout TechniquesHot TemperatureHydrogen-Ion ConcentrationKetoglutaric AcidsKineticsLysineMutationOrnithineOrnithine-Oxo-Acid TransaminasePhylogenyProlineRecombinant Fusion ProteinsRecombinant ProteinsArchaeal ProteinsKetoglutaric AcidsLysineOrnithineOrnithine-Oxo-Acid TransaminaseProlineRecombinant Fusion ProteinsRecombinant Proteinsamino acidaminotransferasearchaeabiosynthesisenzymemetabolismornithineprolinethermophiletransamination

Identifiers

PMID29352105
PMCPMC5846162
OpenAlexW2784969714

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.