Evidence map›Paper›PMID 18658271›Full record

ArticleJournal of bacteriology2008

Identification of sesquiterpene synthases from Nostoc punctiforme PCC 73102 and Nostoc sp. strain PCC 7120.

Sean A Agger, Fernando Lopez-Gallego, Thomas R Hoye, Claudia Schmidt-Dannert

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

39 citing papers in PubMed, 132 citations in OpenAlex.

  1. Review
  2. Terpene biosynthesis in marine sponge animals.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Protein Engineering of a Germacrene A Synthase FromFrontiers in plant science · 2022
    Article
  8. Review
  9. Article
  10. Article
  11. Germacrene A-A Central Intermediate in Sesquiterpene Biosynthesis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Transcriptome Analysis of Oleoresin-Producing TreeFrontiers in plant science · 2018
    Article
  18. Article
  19. Article
  20. Mechanistic investigations on six bacterial terpene cyclases.Beilstein journal of organic chemistry · 2016
    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

4 authors at 1 institution in 1 country.

Sean A AggerDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, 1479 Gortner Avenue, St. Paul, MN 55108, USA.
Fernando Lopez-Gallego
Thomas R Hoye
Claudia Schmidt-Dannert
University of Minnesota · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyanobacteria are a rich source of natural products and are known to produce terpenoids. These bacteria are the major source of the musty-smelling terpenes geosmin and 2-methylisoborneol, which are found in many natural water supplies; however, no terpene synthases have been characterized from these organisms to date. Here, we describe the characterization of three sesquiterpene synthases identified in Nostoc sp. strain PCC 7120 (terpene synthase NS1) and Nostoc punctiforme PCC 73102 (terpene synthases NP1 and NP2). The second terpene synthase in N. punctiforme (NP2) is homologous to fusion-type sesquiterpene synthases from Streptomyces spp. shown to produce geosmin via an intermediate germacradienol. The enzymes were functionally expressed in Escherichia coli, and their terpene products were structurally identified as germacrene A (from NS1), the eudesmadiene 8a-epi-alpha-selinene (from NP1), and germacradienol (from NP2). The product of NP1, 8a-epi-alpha-selinene, so far has been isolated only from termites, in which it functions as a defense compound. Terpene synthases NP1 and NS1 are part of an apparent minicluster that includes a P450 and a putative hybrid two-component protein located downstream of the terpene synthases. Coexpression of P450 genes with their adjacent located terpene synthase genes in E. coli demonstrates that the P450 from Nostoc sp. can be functionally expressed in E. coli when coexpressed with a ferredoxin gene and a ferredoxin reductase gene from Nostoc and that the enzyme oxygenates the NS1 terpene product germacrene A. This represents to the best of our knowledge the first example of functional expression of a cyanobacterial P450 in E. coli.

Indexed as

Alkyl and Aryl TransferasesBacterial ProteinsCloning, MolecularCytochrome P-450 Enzyme SystemEscherichia coliGene ExpressionKineticsNostocOpen Reading FramesRecombinant ProteinsSesquiterpenesAlkyl and Aryl TransferasesBacterial ProteinsCytochrome P-450 Enzyme SystemRecombinant ProteinsSesquiterpenesterpene synthase

Identifiers

PMID18658271
PMCPMC2546793
OpenAlexW2138214147

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.