Evidence map›Paper›PMID 30578862›Full record

ArticleMetabolic engineering2019

Construction of a fusion enzyme for astaxanthin formation and its characterisation in microbial and plant hosts: A new tool for engineering ketocarotenoids.

Marilise Nogueira, Eugenia M A Enfissi, Ralf Welsch, Peter Beyer, Matias D Zurbriggen, Paul D Fraser

Open access · hybridAbstract read
In one paragraph

Article in Metabolic engineering, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

32 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
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  8. Metabolic Engineering ofJournal of fungi (Basel, Switzerland) · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Production of Astaxanthin Using CBFD1/HFBD1 fromBioengineering (Basel, Switzerland) · 2023
    Article
  14. Article
  15. Review
  16. Review
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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

6 authors at 2 institutions in 2 countries.

Marilise NogueiraSchool of Biological Sciences, Royal Holloway University of London, Egham hill, Egham TW200EX, United Kingdom.
Eugenia M A EnfissiSchool of Biological Sciences, Royal Holloway University of London, Egham hill, Egham TW200EX, United Kingdom.
Ralf WelschUniversity of Freiburg, Faculty of Biology II, 79104 Freiburg, Germany.
Peter BeyerUniversity of Freiburg, Faculty of Biology II, 79104 Freiburg, Germany.
Matias D ZurbriggenFaculty of Biology, University of Freiburg and BIOSS Centre for Biological Signalling Studies, University of Freiburg, Schänzlestrasse 18, 79104 Freiburg, Germany.
Paul D FraserSchool of Biological Sciences, Royal Holloway University of London, Egham hill, Egham TW200EX, United Kingdom. Electronic address: p.fraser@rhul.ac.uk.
Royal Holloway University of London · GBUniversity of Freiburg · DE

Funding

Biotechnology and Biological Sciences Research Council BB/P001742/1
6 · The paper itself

Abstract

The high-value ketocarotenoid astaxanthin, a natural red colorant with powerful antioxidant activity, is synthesised from β-carotene by a hydroxylase and an oxygenase enzyme, which perform the addition of two hydroxyl and keto moieties, respectively. Several routes of intermediates, depending on the sequence of action of these enzymes, lead to the formation of astaxanthin. In the present study, the enzyme activities of 3, 3' β-carotene hydroxylase (CRTZ) and 4, 4' β-carotene oxygenase (CRTW) have been combined through the creation of "new to nature" enzyme fusions in order to overcome leakage of non-endogenous intermediates and pleotropic effects associated with their high levels in plants. The utility of flexible linker sequences of varying size has been assessed in the construction of pZ-W enzyme fusions. Frist, in vivo color complementation assays in Escherichia coli have been used to evaluate the potential of the fusion enzymes. Analysis of the carotenoid pigments present in strains generated indicated that the enzyme fusions only possess both catalytic activities when CRTZ is attached as the N-terminal module. Astaxanthin levels in E. coli cells were increased by 1.4-fold when the CRTZ and CRTW enzymes were fused compared to the individual enzymes. Transient expression in Nicotiana benthamiana was then performed in order to assess the potential of the fusions in a plant system. The production of valuable ketocarotenoids was achieved using this plant-based transient expression system. This revealed that CRTZ and CRTW, transiently expressed as a fusion, accumulated similar levels of astaxanthin compared to the expression of the individual enzymes whilst being associated with reduced ketocarotenoid intermediate levels (e.g. phoenicoxanthin, canthaxanthin and 3-OH-echinenone) and a reduced rate of leaf senescence after transformation. Therefore, the quality of the plant material producing the ketocarotenoids was enhanced due to a reduction in the stress induced by the accumulation of high levels of heterologous ketocarotenoid intermediates. The size of the linkers appeared to have no effect upon activity. The potential of the approach to production of valuable plant derived products is discussed.

Indexed as

CarotenoidsEscherichia coliGene FusionKetosesMetabolic EngineeringMixed Function OxygenasesNicotianaPlant LeavesPlantsPlants, Genetically ModifiedPlasmidsXanthophyllsastaxanthinebeta-carotene hydroxylaseCarotenoidsKetosesMixed Function OxygenasesXanthophyllsAstaxanthinFusion enzymeKetocarotenoidsMetabolic engineeringSubstrate channeling

Identifiers

PMID30578862
PMCPMC6374281
OpenAlexW2906201256

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.