Evidence map›Paper›PMID 30526483›Full record

ArticleBMC plant biology2018

Cloning and characterization of norbelladine synthase catalyzing the first committed reaction in Amaryllidaceae alkaloid biosynthesis.

Aparna Singh, Marie-Ange Massicotte, Ariane Garand, Laurence Tousignant, Vincent Ouellette, Gervais Bérubé, Isabel Desgagné-Penix

Abstract read
In one paragraph

Article in BMC plant biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

24 citing papers in PubMed.

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  8. Synthesis, Characterization, and Biological Evaluation ofMolecules (Basel, Switzerland) · 2024
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  12. Emerging functions within the enzyme families of plant alkaloid biosynthesis.Phytochemistry reviews : proceedings of the Phytochemical Society of Europe · 2023
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

7 authors.

Aparna SinghDepartment of Chemistry, Biochemistry and Physics, Université du Québec à Trois-Rivières, 3351 boul. des Forges, Trois-Rivières, QC, G9A 5H7, Canada.
Marie-Ange MassicotteDepartment of Chemistry, Biochemistry and Physics, Université du Québec à Trois-Rivières, 3351 boul. des Forges, Trois-Rivières, QC, G9A 5H7, Canada.
Ariane GarandDepartment of Chemistry, Biochemistry and Physics, Université du Québec à Trois-Rivières, 3351 boul. des Forges, Trois-Rivières, QC, G9A 5H7, Canada.
Laurence TousignantDepartment of Chemistry, Biochemistry and Physics, Université du Québec à Trois-Rivières, 3351 boul. des Forges, Trois-Rivières, QC, G9A 5H7, Canada.
Vincent OuelletteDepartment of Chemistry, Biochemistry and Physics, Université du Québec à Trois-Rivières, 3351 boul. des Forges, Trois-Rivières, QC, G9A 5H7, Canada.
Gervais BérubéDepartment of Chemistry, Biochemistry and Physics, Université du Québec à Trois-Rivières, 3351 boul. des Forges, Trois-Rivières, QC, G9A 5H7, Canada.
Isabel Desgagné-PenixDepartment of Chemistry, Biochemistry and Physics, Université du Québec à Trois-Rivières, 3351 boul. des Forges, Trois-Rivières, QC, G9A 5H7, Canada. Isabel.Desgagne-Penix@uqtr.ca.ORCID http://orcid.org/0000-0002-4355-5503

Funding

Natural Sciences and Engineering Research Council of Canada EQPEQ 472990-2015Natural Sciences and Engineering Research Council of Canada RGPIN 05294-2014
6 · The paper itself

Abstract

backgroundAmaryllidaceae alkaloids (AAs) are a large group of plant-specialized metabolites displaying an array of biological and pharmacological properties. Previous investigations on AA biosynthesis have revealed that all AAs share a common precursor, norbelladine, presumably synthesized by an enzyme catalyzing a Mannich reaction involving the condensation of tyramine and 3,4-dihydroxybenzaldehyde. Similar reactions have been reported. Specifically, norcoclaurine synthase (NCS) which catalyzes the condensation of dopamine and 4-hydroxyphenylacetaldehyde as the first step in benzylisoquinoline alkaloid biosynthesis.

resultsWith the availability of wild daffodil (Narcissus pseudonarcissus) database, a transcriptome-mining search was performed for NCS orthologs. A candidate gene sequence was identified and named norbelladine synthase (NBS). NpNBS encodes for a small protein of 19 kDa with an anticipated pI of 5.5. Phylogenetic analysis showed that NpNBS belongs to a unique clade of PR10/Bet v1 proteins and shared 41% amino acid identity to opium poppy NCS1. Expression of NpNBS cDNA in Escherichia coli produced a recombinant enzyme able to condense tyramine and 3,4-DHBA into norbelladine as determined by high-resolution tandem mass spectrometry.

conclusionsHere, we describe a novel enzyme catalyzing the first committed step of AA biosynthesis, which will facilitate the establishment of metabolic engineering and synthetic biology platforms for the production of AAs.

Indexed as

AmaryllidaceaeAmaryllidaceae AlkaloidsAmino Acid SequenceBenzaldehydesCarbon-Nitrogen LigasesCatecholsCloning, MolecularPhylogenyPlant ProteinsReverse Transcriptase Polymerase Chain ReactionSequence AlignmentTyramineAmaryllidaceae AlkaloidsBenzaldehydesCarbon-Nitrogen LigasesCatecholsnorbelladinenorcoclaurine synthasePlant ProteinsprotocatechualdehydeTyramineAlkaloid biosynthesisAmaryllidaceae alkaloidNarcissus pseudonarcissusNorbelladineNorcoclaurine synthasePathogenesis related protein 10

Identifiers

PMID30526483
PMCPMC6286614

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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.