Evidence map›Paper›PMID 24941968›Full record

ArticleNature communications2014

Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme.

Nethaji J Gallage, Esben H Hansen, Rubini Kannangara, Carl Erik Olsen, Mohammed Saddik Motawia, Kirsten Jørgensen, Inger Holme, Kim Hebelstrup, Michel Grisoni, Birger Lindberg Møller

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
15.6field-weighted citation impact, top 1% 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

64 citing papers in PubMed, 226 citations in OpenAlex.

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4 more citing papers are in PubMed but not listed here.

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

10 authors at 3 institutions in 3 countries.

Nethaji J Gallage1] Plant Biochemistry Laboratory, Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark [2] VILLUM Research Center 'Plant Plasticity', Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark [3] Center for Synthetic Biology: 'bioSYNergy', Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark.
Esben H HansenEvolva A/S, Lersø Parkallé 42-44, 5th floor, DK-2100 Copenhagen, Denmark.
Rubini Kannangara1] Plant Biochemistry Laboratory, Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark [2] VILLUM Research Center 'Plant Plasticity', Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark [3] Center for Synthetic Biology: 'bioSYNergy', Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark.
Carl Erik Olsen1] Plant Biochemistry Laboratory, Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark [2] VILLUM Research Center 'Plant Plasticity', Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark.
Mohammed Saddik Motawia1] Plant Biochemistry Laboratory, Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark [2] VILLUM Research Center 'Plant Plasticity', Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark [3] Center for Synthetic Biology: 'bioSYNergy', Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark.
Kirsten Jørgensen1] Plant Biochemistry Laboratory, Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark [2] VILLUM Research Center 'Plant Plasticity', Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark [3] Center for Synthetic Biology: 'bioSYNergy', Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark.
Inger HolmeAU Flakkebjerg, Danish Centre for Food and Agriculture, University of Aarhus, Forsøgsvej, DK-4200 Slagelse, Denmark.
Kim HebelstrupAU Flakkebjerg, Danish Centre for Food and Agriculture, University of Aarhus, Forsøgsvej, DK-4200 Slagelse, Denmark.
Michel GrisoniCentre de Coopération Internationale en Recherche Agronomique pour le Dévelopement, UMR PVBMT, 97410 Saint Pierre, La Réunion, France.
Birger Lindberg Møller1] Plant Biochemistry Laboratory, Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark [2] VILLUM Research Center 'Plant Plasticity', Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark [3] Center for Synthetic Biology: 'bioSYNergy', Thorvaldsensvej 40, Frederiksberg C, DK-1871 Copenhagen, Denmark [4] Carlsberg Laboratory, Gamle Carlsberg Vej 10, Valby DK-2500, Copenhagen, Denmark.
University of Copenhagen · DKCentre de Coopération Internationale en Recherche Agronomique pour le Développement · FREvolva (Denmark) · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vanillin is a popular and valuable flavour compound. It is the key constituent of the natural vanilla flavour obtained from cured vanilla pods. Here we show that a single hydratase/lyase type enzyme designated vanillin synthase (VpVAN) catalyses direct conversion of ferulic acid and its glucoside into vanillin and its glucoside, respectively. The enzyme shows high sequence similarity to cysteine proteinases and is specific to the substitution pattern at the aromatic ring and does not metabolize caffeic acid and p-coumaric acid as demonstrated by coupled transcription/translation assays. VpVAN localizes to the inner part of the vanilla pod and high transcript levels are found in single cells located a few cell layers from the inner epidermis. Transient expression of VpVAN in tobacco and stable expression in barley in combination with the action of endogenous alcohol dehydrogenases and UDP-glucosyltransferases result in vanillyl alcohol glucoside formation from endogenous ferulic acid. A gene encoding an enzyme showing 71% sequence identity to VpVAN was identified in another vanillin-producing plant species Glechoma hederacea and was also shown to be a vanillin synthase as demonstrated by transient expression in tobacco.

Indexed as

BenzaldehydesBiocatalysisBiosynthetic PathwaysCoumaric AcidsPlant ProteinsVanillaBenzaldehydesCoumaric Acidsferulic acidPlant Proteinsvanillin

Identifiers

PMID24941968
PMCPMC4083428
OpenAlexW2131681747

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.