Evidence map›Paper›PMID 30318713›Full record

ArticleChembiochem : a European journal of chemical biology2019

Structure and Catalytic Mechanism of a Bacterial Friedel-Crafts Acylase.

Tea Pavkov-Keller, Nina G Schmidt, Anna Żądło-Dobrowolska, Wolfgang Kroutil, Karl Gruber

Open access · hybridAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed, 33 citations in OpenAlex.

  1. Biocatalytic Regioselective C-Formylation of Resorcinol Derivatives.Angewandte Chemie (International ed. in English) · 2026
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  5. Review
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  7. Article
  8. Microorganisms · 2022
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. CariogenicACS infectious diseases · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. The steroid side-chain-cleaving aldolase Ltp2-ChsH2The Journal of biological chemistry · 2019
    Article
  18. Structure and Catalytic Mechanism of a Bacterial Friedel-Crafts Acylase.Chembiochem : a European journal of chemical biology · 2019
    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.

Tea Pavkov-KellerAustrian Centre of Industrial Biotechnology (ACIB), Petersgasse 14, 8010, Graz, Austria.ORCID 0000-0001-7871-6680
Nina G SchmidtAustrian Centre of Industrial Biotechnology (ACIB), Petersgasse 14, 8010, Graz, Austria.
Anna Żądło-DobrowolskaDepartment of Chemistry, Organic and Bioorganic Chemistry, University of Graz, Heinrichstrasse 28/2, 8010, Graz, Austria.ORCID 0000-0003-4240-9851
Wolfgang KroutilAustrian Centre of Industrial Biotechnology (ACIB), Petersgasse 14, 8010, Graz, Austria.ORCID 0000-0002-2151-6394
Karl GruberAustrian Centre of Industrial Biotechnology (ACIB), Petersgasse 14, 8010, Graz, Austria.ORCID 0000-0002-3485-9740
University of Graz · AT

Funding

Austrian Science Fund FWF M 2172Austrian Science Fund FWF P 29432
6 · The paper itself

Abstract

C-C bond-forming reactions are key transformations for setting up the carbon frameworks of organic compounds. In this context, Friedel-Crafts acylation is commonly used for the synthesis of aryl ketones, which are common motifs in many fine chemicals and natural products. A bacterial multicomponent acyltransferase from Pseudomonas protegens (PpATase) catalyzes such Friedel-Crafts C-acylation of phenolic substrates in aqueous solution, reaching up to >99 % conversion without the need for CoA-activated reagents. We determined X-ray crystal structures of the native and ligand-bound complexes. This multimeric enzyme consists of three subunits: PhlA, PhlB, and PhlC, arranged in a Phl(A

Indexed as

AcylationAcyltransferasesBacterial ProteinsBiocatalysisCrystallography, X-RayMutagenesis, Site-DirectedMutationPhloroglucinolProtein BindingProtein SubunitsPseudomonasAcyltransferasesBacterial ProteinsmonoacetylphloroglucinolPhloroglucinolProtein SubunitsacyltransferasesFriedel-Crafts acylationmulticomponent enzymessolid-state structurestransferasesX-ray diffraction

Identifiers

PMID30318713
PMCPMC6392133
OpenAlexW2896736304

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.