Evidence map›Paper›PMID 31086389›Full record

ArticlePloS one2019

Construction of a pathway to C50-ε-carotene.

Yusuke Otani, Takashi Maoka, Shigeko Kawai-Noma, Kyoichi Saito, Daisuke Umeno

Abstract read
In one paragraph

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Recent advances in carotenoid absorption, distribution, and elimination.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2025
    Review
  2. 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

5 authors.

Yusuke OtaniDepartment of Applied Chemistry and Biotechnology, Chiba University, Chiba, Japan.
Takashi MaokaResearch Institute for Production Development, Kyoto, Japan.
Shigeko Kawai-NomaDepartment of Applied Chemistry and Biotechnology, Chiba University, Chiba, Japan.
Kyoichi SaitoDepartment of Applied Chemistry and Biotechnology, Chiba University, Chiba, Japan.
Daisuke UmenoDepartment of Applied Chemistry and Biotechnology, Chiba University, Chiba, Japan.ORCID 0000-0001-8107-552X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Substrate tolerance of bacterial cyclases has been demonstrated in various contexts, but little is known about that of plant cyclases. Here, we tested two plant ε-cyclases to convert C50-lycopene, which we previously established by rounds of directed evolution. Unlike bacterial β-cyclases, two-end cyclase from lettuce exhibited complete specificity against this molecule, indicating that this enzyme has some mechanism that exerts size-specificity. Arabidopsis one-end cyclase At-y2 showed detectable activity to C50-lycopene. Interestingly, we found that it functions as a two-end cyclase in a C50 context. Based on this observation, a possible model for substrate discrimination of this enzyme is proposed.

Indexed as

Metabolic EngineeringArabidopsisCarotenoidsLyasesSubstrate SpecificityCarotenoidsLyases

Identifiers

PMID31086389
PMCPMC6516660

What OpenQuestion holds

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LicenceCC BY
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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.