Evidence map›Paper›PMID 31444322›Full record

ArticleNature communications2019

Orthogonal monoterpenoid biosynthesis in yeast constructed on an isomeric substrate.

Codruta Ignea, Morten H Raadam, Mohammed S Motawia, Antonios M Makris, Claudia E Vickers, Sotirios C Kampranis

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

46 citing papers in PubMed, 138 citations in OpenAlex.

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  9. The cis-prenyltransferase protein family in Taraxacum koksaghyz.The Plant journal : for cell and molecular biology · 2025
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  16. Engineering peroxisomal biosynthetic pathways for maximization of triterpene production inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Biomimetic Approach to Diverse Coral Diterpenes from a Biosynthetic Scaffold.Angewandte Chemie (International ed. in English) · 2023
    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

6 authors at 3 institutions in 3 countries.

Codruta IgneaBiochemical Engineering Group, Plant Biochemistry Section, Department of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej 40, 1871, Frederiksberg C, Denmark.ORCID http://orcid.org/0000-0002-6304-9413
Morten H RaadamBiochemical Engineering Group, Plant Biochemistry Section, Department of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej 40, 1871, Frederiksberg C, Denmark.ORCID http://orcid.org/0000-0002-6796-0079
Mohammed S MotawiaBiochemical Engineering Group, Plant Biochemistry Section, Department of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej 40, 1871, Frederiksberg C, Denmark.ORCID http://orcid.org/0000-0001-5582-9463
Antonios M MakrisInstitute of Applied Biosciences - Centre for Research and Technology Hellas (INAB-CERTH), 57001, Thermi, Thessaloniki, Greece.
Claudia E VickersAustralian Institute for Bioengineering and Nanotechnology (AIBN), University of Queensland, St. Lucia, QLD 4072, Australia.ORCID http://orcid.org/0000-0002-0792-050X
Sotirios C KampranisBiochemical Engineering Group, Plant Biochemistry Section, Department of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej 40, 1871, Frederiksberg C, Denmark. soka@plen.ku.dk.
University of Copenhagen · DKCentre for Research and Technology Hellas · GRCommonwealth Scientific and Industrial Research Organisation · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synthetic biology efforts for the production of valuable chemicals are frequently hindered by the structure and regulation of the native metabolic pathways of the chassis. This is particularly evident in the case of monoterpenoid production in Saccharomyces cerevisiae, where the canonical terpene precursor geranyl diphosphate is tightly coupled to the biosynthesis of isoprenoid compounds essential for yeast viability. Here, we establish a synthetic orthogonal monoterpenoid pathway based on an alternative precursor, neryl diphosphate. We identify structural determinants of isomeric substrate selectivity in monoterpene synthases and engineer five different enzymes to accept the alternative substrate with improved efficiency and specificity. We combine the engineered enzymes with dynamic regulation of metabolic flux to harness the potential of the orthogonal substrate and improve the production of industrially-relevant monoterpenes by several-fold compared to the canonical pathway. This approach highlights the introduction of synthetic metabolism as an effective strategy for high-value compound production.

Indexed as

Metabolic EngineeringBiosynthetic PathwaysIntramolecular LyasesIsomerismMonoterpenesMutagenesis, Site-DirectedPolyisoprenyl PhosphatesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificitySynthetic Biologygeranyl pyrophosphateIntramolecular LyasesMonoterpenespinene cyclase IPolyisoprenyl PhosphatesSaccharomyces cerevisiae Proteins

Identifiers

PMID31444322
PMCPMC6707142
OpenAlexW2969469154

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.