Evidence map›Paper›PMID 22415272›Full record

ArticleThe Plant cell2012

Lysine decarboxylase catalyzes the first step of quinolizidine alkaloid biosynthesis and coevolved with alkaloid production in leguminosae.

Somnuk Bunsupa, Kae Katayama, Emi Ikeura, Akira Oikawa, Kiminori Toyooka, Kazuki Saito, Mami Yamazaki

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2012. 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
10.4field-weighted citation impact, top 2% 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, 146 citations in OpenAlex.

  1. Ancient origins of alkaloid biosynthesis in medicinal clubmosses.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Physiological and Metabolic Responses of Wheat (ACS agricultural science & technology · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Development of phytochemical genomics: From decoding metabolome to functional genomics and biotechnology of plant metabolism.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2025
    Review
  11. De Novo Transcriptome Assembly of Cedar (Current issues in molecular biology · 2024
    Article
  12. Review
  13. Emerging functions within the enzyme families of plant alkaloid biosynthesis.Phytochemistry reviews : proceedings of the Phytochemical Society of Europe · 2023
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. A Pyridine Dearomatization Approach to the Matrine-Type Lupin Alkaloids.Journal of the American Chemical Society · 2022
    Article

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

7 authors at 2 institutions in 1 country.

Somnuk BunsupaGraduate School of Pharmaceutical Sciences, Chiba University, Chuo-ku, Chiba 260-8675, Japan.
Kae Katayama
Emi Ikeura
Akira Oikawa
Kiminori Toyooka
Kazuki Saito
Mami Yamazaki
Chiba University · JPRIKEN Center for Sustainable Resource Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine decarboxylase (LDC) catalyzes the first-step in the biosynthetic pathway of quinolizidine alkaloids (QAs), which form a distinct, large family of plant alkaloids. A cDNA of lysine/ornithine decarboxylase (L/ODC) was isolated by differential transcript screening in QA-producing and nonproducing cultivars of Lupinus angustifolius. We also obtained L/ODC cDNAs from four other QA-producing plants, Sophora flavescens, Echinosophora koreensis, Thermopsis chinensis, and Baptisia australis. These L/ODCs form a phylogenetically distinct subclade in the family of plant ornithine decarboxylases. Recombinant L/ODCs from QA-producing plants preferentially or equally catalyzed the decarboxylation of L-lysine and L-ornithine. L. angustifolius L/ODC (La-L/ODC) was found to be localized in chloroplasts, as suggested by the transient expression of a fusion protein of La-L/ODC fused to the N terminus of green fluorescent protein in Arabidopsis thaliana. Transgenic tobacco (Nicotiana tabacum) suspension cells and hairy roots produced enhanced levels of cadaverine-derived alkaloids, and transgenic Arabidopsis plants expressing (La-L/ODC) produced enhanced levels of cadaverine, indicating the involvement of this enzyme in lysine decarboxylation to form cadaverine. Site-directed mutagenesis and protein modeling studies revealed a structural basis for preferential LDC activity, suggesting an evolutionary implication of L/ODC in the QA-producing plants.

Indexed as

AlkaloidsArabidopsisCadaverineCarboxy-LyasesChloroplastsCloning, MolecularDecarboxylationLupinusModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNicotianaOrnithine DecarboxylasePlant ProteinsPlants, Genetically ModifiedQuinolizidinesAlkaloidsCadaverineCarboxy-Lyaseslysine decarboxylaseOrnithine DecarboxylasePlant ProteinsQuinolizidines

Identifiers

PMID22415272
PMCPMC3336119
OpenAlexW2146186017

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.