Evidence map›Paper›PMID 35446557›Full record

ArticleACS chemical biology2022

Identification and Characterization of Bifunctional Drimenol Synthases of Marine Bacterial Origin.

Nhu Ngoc Quynh Vo, Yuhta Nomura, Kiyomi Kinugasa, Hiroshi Takagi, Shunji Takahashi

Open access · hybridAbstract read
In one paragraph

Article in ACS chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. The evolutionary history and modern diversity of triterpenoid cyclases.bioRxiv : the preprint server for biology · 2025
    Article
  8. Crystal structure and catalytic mechanism of drimenol synthase, an unusual bifunctional terpene cyclase-phosphatase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Review
  10. Unusual Sesquiterpenes fromJournal of natural products · 2024
    Article
  11. Review
  12. Article
  13. Discovery, Structure, and Mechanism of a Class II Sesquiterpene Cyclase.Journal of the American Chemical Society · 2022
    Article
  14. Article
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 1 institution in 1 country.

Nhu Ngoc Quynh VoNatural Product Biosynthesis Research Unit, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.ORCID 0000-0002-7522-9761
Yuhta NomuraBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.ORCID 0000-0002-4954-4653
Kiyomi KinugasaNatural Product Biosynthesis Research Unit, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Hiroshi TakagiNatural Product Biosynthesis Research Unit, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Shunji TakahashiNatural Product Biosynthesis Research Unit, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.ORCID 0000-0003-1684-9298
RIKEN Center for Sustainable Resource Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Natural drimane-type sesquiterpenes, including drimenol, display diverse biological activities. These active compounds are distributed in plants and fungi; however, their accumulation in bacteria remains unknown. Consequently, bacterial drimane-type sesquiterpene synthases remain to be characterized. Here, we report five drimenol synthases (DMSs) of marine bacterial origin, all belonging to the haloacid dehalogenase (HAD)-like hydrolase superfamily with the conserved DDxxE motif typical of class I terpene synthases and the DxDTT motif found in class II diterpene synthases. They catalyze two continuous reactions: the cyclization of farnesyl pyrophosphate (FPP) into drimenyl pyrophosphate and dephosphorylation of drimenyl pyrophosphate into drimenol. Protein structure modeling of the characterized

Indexed as

Alkyl and Aryl TransferasesSesquiterpenesAspartic AcidDiphosphatesGenes, BacterialPolycyclic SesquiterpenesAlkyl and Aryl TransferasesAspartic AcidDiphosphatesdrimenolPolycyclic SesquiterpenesSesquiterpenes

Identifiers

PMID35446557
PMCPMC9128629
OpenAlexW4224275923

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.