Evidence map›Paper›PMID 35704353›Full record

ArticleThe FEBS journal2022

Molecular characterization of cyanobacterial short-chain prenyltransferases and discovery of a novel GGPP phosphatase.

Alessandro Satta, Lygie Esquirol, Birgitta E Ebert, Janet Newman, Thomas S Peat, Manuel Plan, Gerhard Schenk, Claudia E Vickers

Open access · hybridAbstract read
In one paragraph

Article in The FEBS journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

8 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. CyanoCyc cyanobacterial web portal.Frontiers in microbiology · 2024
    Article
  6. Article
  7. Review
  8. 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

8 authors at 3 institutions in 1 country.

Alessandro SattaAustralian Institute for Bioengineering and Biotechnology, The University of Queensland, St. Lucia, Australia.ORCID 0000-0002-1544-7230
Lygie EsquirolCentre for Cell Factories and Biopolymers, Griffith Institute for Drug Discovery, Griffith University, Nathan, Australia.
Birgitta E EbertAustralian Institute for Bioengineering and Biotechnology, The University of Queensland, St. Lucia, Australia.ORCID 0000-0001-9425-7509
Janet NewmanCSIRO Biomedical Program, Parkville, Australia.
Thomas S PeatCSIRO Biomedical Program, Parkville, Australia.
Manuel PlanMetabolomics Australia (Queensland Node), Australian Institute for Bioengineering and Nanotechnology, The University of Queensland, St. Lucia, Australia.
Gerhard SchenkAustralian Institute for Bioengineering and Biotechnology, The University of Queensland, St. Lucia, Australia.
Claudia E VickersCSIRO Synthetic Biology Future Science Platform, Brisbane, Australia.
Commonwealth Scientific and Industrial Research Organisation · AUThe University of Queensland · AUGriffith University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyanobacteria are photosynthetic prokaryotes with strong potential to be used for industrial terpenoid production. However, the key enzymes forming the principal terpenoid building blocks, called short-chain prenyltransferases (SPTs), are insufficiently characterized. Here, we examined SPTs in the model cyanobacteria Synechococcus elongatus sp. PCC 7942 and Synechocystis sp. PCC 6803. Each species has a single putative SPT (SeCrtE and SyCrtE, respectively). Sequence analysis identified these as type-II geranylgeranyl pyrophosphate synthases (GGPPSs) with high homology to GGPPSs found in the plastids of green plants and other photosynthetic organisms. In vitro analysis demonstrated that SyCrtE is multifunctional, producing geranylgeranyl pyrophosphate (GGPP; C

Indexed as

DimethylallyltranstransferaseSynechococcusGeranylgeranyl-Diphosphate GeranylgeranyltransferasePhosphoric Monoester HydrolasesPolyisoprenyl PhosphatesDimethylallyltranstransferaseGeranylgeranyl-Diphosphate Geranylgeranyltransferasegeranylgeranyl pyrophosphatePhosphoric Monoester HydrolasesPolyisoprenyl PhosphatescarotenoidsgeranylgeraniolisoprenoidsMEP pathwayphotosynthesisprenyl phosphate

Identifiers

PMID35704353
PMCPMC9796789
OpenAlexW4282966296

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.