Evidence map›Paper›PMID 25996186›Full record

ReviewBioengineered2015

Bacterial d-amino acid oxidases: Recent findings and future perspectives.

Shouji Takahashi, Katsumasa Abe, Yoshio Kera

Open access · goldAbstract readReview
In one paragraph

Review in Bioengineered, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

18 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. d-Amino Acids Are Exuded by Arabidopsis thaliana Roots to the Rhizosphere.International journal of molecular sciences · 2018
    Article
  15. Article
  16. Article
  17. Review
  18. 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

3 authors at 2 institutions in 1 country.

Shouji Takahashia Department of Bioengineering ; Nagaoka University of Technology ; Nagaoka , Niigata , Japan.
Katsumasa Abe
Yoshio Kera
Nagaoka University · JPNagaoka University of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

D-Amino acid oxidase (DAO) is a flavin enzyme that catalyzes the oxidative deamination of d-amino acids. This enzyme has been studied extensively both biochemically and structurally as a model for the oxidase-dehydrogenase class of flavoproteins. This enzyme also has various applications, such as the determination of d-amino acids and production of building blocks for a number of pharmaceuticals. DAO has been found mainly in eukaryotic organisms and has been suggested to play a significant role in various cellular processes, one of which includes neurotransmission in the human brain. In contrast, this enzyme has not been identified in prokaryotic organisms. Some studies have recently identified and characterized DAO enzyme in some actinobacteria. In addition, a genome database search reveals a wide distribution of DAO homologous genes in this bacterial group. The bacterial DAOs characterized so far have certain distinct properties in comparison to eukaryotic DAOs. These enzymes also exhibit some important applicable properties, suggesting that bacteria could be used as a source for obtaining novel and useful DAOs. The physiological function of bacterial DAO have been proposed to include the degradation of non-canonical d-amino acids released from cell wall, but is still largely unknown and need to be studied in depth.

Indexed as

Amino AcidsBacteriaBacterial ProteinsBiotechnologyBrainD-Amino-Acid OxidaseEnzyme StabilityFlavoproteinsHumansKineticsNerve Tissue ProteinsRecombinant ProteinsSpecies SpecificitySubstrate SpecificitySynaptic TransmissionAmino AcidsBacterial ProteinsD-Amino-Acid OxidaseFlavoproteinsNerve Tissue ProteinsRecombinant Proteinsbacteriad-amino acid oxidaseenzymatic propertiesflavin enzymephysiological rolepotential applicationsstructure

Identifiers

PMID25996186
PMCPMC4601262
OpenAlexW1568430388

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.