Evidence map›Paper›PMID 26659564›Full record

ArticlePloS one2015

Diversity of ABBA Prenyltransferases in Marine Streptomyces sp. CNQ-509: Promiscuous Enzymes for the Biosynthesis of Mixed Terpenoid Compounds.

Franziska Leipoldt, Philipp Zeyhle, Andreas Kulik, Jörn Kalinowski, Lutz Heide, Leonard Kaysser

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. 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
2.6field-weighted citation impact, top 10% 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, 30 citations in OpenAlex.

  1. MAR4Journal of natural products · 2024
    Review
  2. Review
  3. Bacterial terpenome.Natural product reports · 2021
    Review
  4. Article
  5. Article
  6. Review
  7. Enzymatic studies on aromatic prenyltransferases.Journal of natural medicines · 2020
    Review
  8. Article
  9. Article
  10. Article
  11. Asymmetric Alkene and Arene Halofunctionalization Reactions in Meroterpenoid Biosynthesis.Synlett : accounts and rapid communications in synthetic organic chemistry · 2018
    Article
  12. Article
  13. 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

6 authors at 3 institutions in 1 country.

Franziska LeipoldtPharmaceutical Biology, Pharmaceutical Institute, Eberhard Karls University Tübingen, Tübingen, Germany.
Philipp ZeyhlePharmaceutical Biology, Pharmaceutical Institute, Eberhard Karls University Tübingen, Tübingen, Germany.
Andreas KulikMicrobial Biotechnology, Interfaculty Institute of Microbiology and Infection Medicine, Eberhard Karls University Tübingen, Tübingen, Germany.
Jörn KalinowskiMicrobial Genomics and Biotechnology, Center for Biotechnology, Bielefeld University, Bielefeld, Germany.
Lutz HeidePharmaceutical Biology, Pharmaceutical Institute, Eberhard Karls University Tübingen, Tübingen, Germany.
Leonard KaysserPharmaceutical Biology, Pharmaceutical Institute, Eberhard Karls University Tübingen, Tübingen, Germany.
German Center for Infection Research · DEUniversity of Tübingen · DEBielefeld University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Terpenoids are arguably the largest and most diverse family of natural products, featuring prominently in e.g. signalling, self-defence, UV-protection and electron transfer. Prenyltransferases are essential players in terpenoid and hybrid isoprenoid biosynthesis that install isoprene units on target molecules and thereby often modulate their bioactivity. In our search for new prenyltransferase biocatalysts we focused on the marine-derived Streptomyces sp. CNQ-509, a particularly rich source of meroterpenoid chemistry. Sequencing and analysis of the genome of Streptomyces sp. CNQ-509 revealed seven putative phenol/phenazine-specific ABBA prenyltransferases, and one putative indole-specific ABBA prenyltransferase. To elucidate the substrate specificity of the ABBA prenyltransferases and to learn about their role in secondary metabolism, CnqP1 -CnqP8 were produced in Escherichia coli and incubated with various aromatic and isoprenoid substrates. Five of the eight prenyltransferases displayed enzymatic activity. The efficient conversion of dihydroxynaphthalene derivatives by CnqP3 (encoded by AA958_24325) and the co-location of AA958_24325 with genes characteristic for the biosynthesis of THN (tetrahydroxynaphthalene)-derived natural products indicates that the enzyme is involved in the formation of debromomarinone or other naphthoquinone-derived meroterpenoids. Moreover, CnqP3 showed high flexibility towards a range of aromatic and isoprenoid substrates and thus represents an interesting new tool for biocatalytic applications.

Indexed as

Amino Acid SequenceDimethylallyltranstransferaseMass SpectrometryMolecular StructureNaphtholsPrenylationProtein Structure, SecondaryStreptomycesSubstrate SpecificityTerpenesDimethylallyltranstransferaseNaphtholsTerpenes

Identifiers

PMID26659564
PMCPMC4684245
OpenAlexW2221017522

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.