Evidence map›Paper›PMID 41257072›Full record

ArticlePlant biotechnology (Tokyo, Japan)2025

CYP71D8 and CYP82A2 catalyze the last committed step in biosynthesis of glyceollin isomers in soybean.

Tomoyoshi Akashi, Kai Uchida, Toshio Aoki

Abstract read
In one paragraph

Article in Plant biotechnology (Tokyo, Japan), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

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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

3 citing papers in PubMed.

  1. Discovery of pseudobaptigenin synthase in fungal-infected Trifolium pratense roots.The Plant journal : for cell and molecular biology · 2026
    Article
  2. Article
  3. 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

3 authors.

Tomoyoshi AkashiDepartment of Applied Biological Sciences, Nihon University, Fujisawa, Kanagawa 252-0880, Japan.
Kai UchidaDepartment of Applied Biological Sciences, Nihon University, Fujisawa, Kanagawa 252-0880, Japan.
Toshio AokiDepartment of Applied Biological Sciences, Nihon University, Fujisawa, Kanagawa 252-0880, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glyceollins, which are prenylated pterocarpan phytoalexins found in soybean, play important roles in plant-microbe interactions. During biosynthesis, the formation of the cyclic ether ring from the C-5 prenyl side chain provides structural diversity to the glyceollin isomers. This reaction has been attributed to cytochrome P450 (P450); however, it is unclear whether a single enzyme or multiple enzymes are involved in glyceollin isomer formation. In this study, we searched a co-expressed gene network database for soybean. Known genes involved in glyceollin biosynthesis were used as queries, and eight P450s (CYP71D8, CYP81E24, CYP82A2, CYP82A3, CYP82A4, CYP93A2, CYP93A3, and CYP736A33) were selected as candidates. In vitro enzyme assays using recombinant yeast microsomes expressing P450s revealed that CYP71D8 produced glyceollin I from 4-dimethylallylglycinol, and CYP82A2 yielded glyceollin III from 2-dimethylallylglycinol. Real-time PCR analysis showed that transcripts of

Indexed as

cytochrome P450glyceollinGlycine maxphytoalexin

Identifiers

PMID41257072
PMCPMC12622905

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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.