Evidence map›Paper›PMID 17056707›Full record

ArticleThe Plant cell2006

Branched-chain aminotransferase4 is part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates in Arabidopsis.

Joachim Schuster, Tanja Knill, Michael Reichelt, Jonathan Gershenzon, Stefan Binder

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

85 citing papers in PubMed, 196 citations in OpenAlex.

  1. Article
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  5. Review
  6. Review
  7. Transcriptional activation ofFrontiers in plant science · 2025
    Article
  8. Article
  9. Effect of sodium selenite on the synthesis of glucosinolates and antioxidant capacity in Chinese cabbage (Physiology and molecular biology of plants : an international journal of functional plant biology · 2024
    Article
  10. Article
  11. Natural Products That Contain Higher Homologated Amino Acids.Chembiochem : a European journal of chemical biology · 2024
    Review
  12. Article
  13. Review
  14. Article
  15. Transcriptome Dynamics ofInternational journal of molecular sciences · 2023
    Article
  16. Review
  17. Article
  18. Article
  19. Genetic Improvement ofPlants (Basel, Switzerland) · 2023
    Review
  20. Article

25 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

5 authors at 2 institutions in 1 country.

Joachim SchusterMolekulare Botanik, Universität Ulm, 89069 Ulm, Germany.
Tanja Knill
Michael Reichelt
Jonathan Gershenzon
Stefan Binder
Universität Ulm · DEMax Planck Institute for Chemical Ecology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As part of our analysis of branched-chain amino acid metabolism in plants, we analyzed the function of Arabidopsis thaliana BRANCHED-CHAIN AMINOTRANSFERASE4 (BCAT4). Recombinant BCAT4 showed high efficiency with Met and its derivatives and the corresponding 2-oxo acids, suggesting its participation in the chain elongation pathway of Met-derived glucosinolate biosynthesis. This was substantiated by in vivo analysis of two BCAT4 T-DNA knockout mutants, in which Met-derived aliphatic glucosinolate accumulation is reduced by approximately 50%. The increase in free Met and S-methylmethionine levels in these mutants, together with in vitro substrate specificity, strongly implicate BCAT4 in catalysis of the initial deamination of Met to 4-methylthio-2-oxobutyrate. BCAT4 transcription is induced by wounding and is predominantly observed in the phloem. BCAT4 transcript accumulation also follows a diurnal rhythm, and green fluorescent protein tagging experiments and subcellular protein fractions show that BCAT4 is located in the cytosol. The assignment of BCAT4 to the Met chain elongation pathway documents the close evolutionary relationship of this pathway to Leu biosynthesis. In addition to BCAT4, the enzyme methylthioalkylmalate synthase 1 has been recruited for the Met chain elongation pathway from a gene family involved in Leu formation. This suggests that the two pathways have a common evolutionary origin.

Indexed as

ArabidopsisBase SequenceCatalysisDNA, PlantDNA PrimersGlucosinolatesLightMethionineMolecular Sequence DataMutagenesisPromoter Regions, GeneticRNA, MessengerSubstrate SpecificityTransaminasesbranched-chain-amino-acid transaminaseDNA, PlantDNA PrimersGlucosinolatesMethionineRNA, MessengerTransaminases

Identifiers

PMID17056707
PMCPMC1626624
OpenAlexW2172276499

What OpenQuestion holds

Textmetadata
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.