Evidence map›Paper›PMID 25620969›Full record

ArticleFrontiers in plant science2014

Garlic γ-glutamyl transpeptidases that catalyze deglutamylation of biosynthetic intermediate of alliin.

Naoko Yoshimoto, Ayami Yabe, Yuka Sugino, Soichiro Murakami, Niti Sai-Ngam, Shin-Ichiro Sumi, Tadamitsu Tsuneyoshi, Kazuki Saito

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
6.2field-weighted citation impact, top 4% 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

26 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Identification of S-1-propenyl-Food chemistry. Molecular sciences · 2025
    Article
  5. 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
  6. Article
  7. Overlooked and misunderstood: can glutathione conjugates be clues to understanding plant glutathione transferases?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  8. Article
  9. Article
  10. Understanding the defense mechanism ofFrontiers in plant science · 2024
    Article
  11. Effect of Thermal Processes onFoods (Basel, Switzerland) · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Review
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

8 authors at 3 institutions in 1 country.

Naoko YoshimotoGraduate School of Pharmaceutical Sciences, Chiba University Chiba, Japan.
Ayami YabeGraduate School of Pharmaceutical Sciences, Chiba University Chiba, Japan.
Yuka SuginoGraduate School of Pharmaceutical Sciences, Chiba University Chiba, Japan.
Soichiro MurakamiGraduate School of Pharmaceutical Sciences, Chiba University Chiba, Japan.
Niti Sai-NgamGraduate School of Pharmaceutical Sciences, Chiba University Chiba, Japan.
Shin-Ichiro SumiResearch Planning Department, Wakunaga Pharmaceutical Company Akitakata, Japan.
Tadamitsu TsuneyoshiCentral Research Institute, Wakunaga Pharmaceutical Company Akitakata, Japan.
Kazuki SaitoGraduate School of Pharmaceutical Sciences, Chiba University Chiba, Japan ; RIKEN Center for Sustainable Resource Science Yokohama, Japan.
Chiba University · JPWakunaga (Japan) · JPRIKEN Center for Sustainable Resource Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

S-Alk(en)yl-L-cysteine sulfoxides are pharmaceutically important secondary metabolites produced by plants that belong to the genus Allium. Biosynthesis of S-alk(en)yl-L-cysteine sulfoxides is initiated by S-alk(en)ylation of glutathione, which is followed by the removal of glycyl and γ-glutamyl groups and S-oxygenation. However, most of the enzymes involved in the biosynthesis of S-alk(en)yl-L-cysteine sulfoxides in Allium plants have not been identified. In this study, we identified three genes, AsGGT1, AsGGT2, and AsGGT3, from garlic (Allium sativum) that encode γ-glutamyl transpeptidases (GGTs) catalyzing the removal of the γ-glutamyl moiety from a putative biosynthetic intermediate of S-allyl-L-cysteine sulfoxide (alliin). The recombinant proteins of AsGGT1, AsGGT2, and AsGGT3 exhibited considerable deglutamylation activity toward a putative alliin biosynthetic intermediate, γ-glutamyl-S-allyl-L-cysteine, whereas these proteins showed very low deglutamylation activity toward another possible alliin biosynthetic intermediate, γ-glutamyl-S-allyl-L-cysteine sulfoxide. The deglutamylation activities of AsGGT1, AsGGT2, and AsGGT3 toward γ-glutamyl-S-allyl-L-cysteine were elevated in the presence of the dipeptide glycylglycine as a γ-glutamyl acceptor substrate, although these proteins can act as hydrolases in the absence of a proper acceptor substrate, except water. The apparent K m values of AsGGT1, AsGGT2, and AsGGT3 for γ-glutamyl-S-allyl-L-cysteine were 86 μM, 1.1 mM, and 9.4 mM, respectively. Subcellular distribution of GFP-fusion proteins transiently expressed in onion cells suggested that AsGGT2 localizes in the vacuole, whereas AsGGT1 and AsGGT3 possess no apparent transit peptide for localization to intracellular organelles. The different kinetic properties and subcellular localizations of AsGGT1, AsGGT2, and AsGGT3 suggest that these three GGTs may contribute differently to the biosynthesis of alliin in garlic.

Indexed as

alliindeglutamylationgarlicsecondary metabolismγ-glutamyl transpeptidase

Identifiers

PMID25620969
PMCPMC4288057
OpenAlexW2087943237

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.