Evidence map›Paper›PMID 39314172›Full record

ArticleChembiochem : a European journal of chemical biology2024

Cavity-Based Discovery of New Fatty Acid Photodecarboxylases.

Stefan Simić, Marco Cespugli, Michael C Hetmann, Ursula Kahler, Valentina Jurkaš, Marikagiusy Di Giacomo, Maria E Russo, Antonio Marzocchella, Christian C Gruber, Bettina M Nestl and 2 more

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Cavity-Based Discovery of New Fatty Acid Photodecarboxylases.Chembiochem : a European journal of chemical biology · 2024
    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

12 authors.

Stefan SimićInstitute of Chemistry, University of Graz, Heinrichstraße 28, 8010, Graz, Austria.ORCID 0000-0002-8226-8881
Marco CespugliInnophore GmbH, Am Eisernen Tor 3, 8010, Graz, Austria.
Michael C HetmannInnophore GmbH, Am Eisernen Tor 3, 8010, Graz, Austria.ORCID 0000-0002-4726-7197
Ursula KahlerInnophore GmbH, Am Eisernen Tor 3, 8010, Graz, Austria.
Valentina JurkašInstitute of Chemistry, University of Graz, Heinrichstraße 28, 8010, Graz, Austria.ORCID 0000-0001-7464-240X
Marikagiusy Di GiacomoDipartimento di Ingegneria Chimica dei Materiali e della Produzione Industriale, Università degli Studi di Napoli Federico II, P.le V. Tecchio 80, 80125, Napoli, Italy.
Maria E RussoCNR-Istituto di Scienze Tecnologie per l'Energia e la Mobilità Sostenibili, P.le V. Tecchio 80, 80125, Napoli, Italy.ORCID 0000-0002-5920-0096
Antonio MarzocchellaDipartimento di Ingegneria Chimica dei Materiali e della Produzione Industriale, Università degli Studi di Napoli Federico II, P.le V. Tecchio 80, 80125, Napoli, Italy.ORCID 0000-0002-8124-9419
Christian C GruberInnophore GmbH, Am Eisernen Tor 3, 8010, Graz, Austria.ORCID 0000-0003-0214-449X
Bettina M NestlInnophore GmbH, Am Eisernen Tor 3, 8010, Graz, Austria.ORCID 0000-0003-1282-195X
Christoph K WinklerInstitute of Chemistry, University of Graz, Heinrichstraße 28, 8010, Graz, Austria.ORCID 0000-0003-3068-9817
Wolfgang KroutilInstitute of Chemistry, University of Graz, Heinrichstraße 28, 8010, Graz, Austria.ORCID 0000-0002-2151-6394

Funding

European Union's Horizon 764920Horizon 2020 Research and Innovation Program 862081
6 · The paper itself

Abstract

Light-dependent fatty acid photodecarboxylases (FAPs) hold significant potential for biotechnology, due to their capability to produce alka(e)nes directly from the corresponding (un)saturated natural fatty acids requiring light as the only reagent. This study expands the family of FAPs through cavity-based enzyme discovery methods. Thirty enzyme candidates with potential photodecarboxylation activity were identified by matching the cavities of four related template structures against the Protein Data Bank's flavoproteins, a library of proteins identified via the Foldseek Search Server, and homology models of sequences resulting from BLAST. Subsequent docking experiments narrowed this library to ten promising enzymes, which were expressed and assessed in vitro, identifying four photodecarboxylases. Out of these enzymes, the GMC oxidoreductase from Coccomyxa sp. Obi (CoFAP) was characterized in detail, which revealed high activity in the decarboxylation reactions of palmitic acid and octanoic acid and a broad pH tolerance (pH 6.5-9.5).

Indexed as

Carboxy-LyasesFatty AcidsCaprylatesHydrogen-Ion ConcentrationMolecular Docking SimulationPalmitic AcidCaprylatesCarboxy-LyasesFatty Acidsoctanoic acidPalmitic AcidBiocatalysisEnzyme discoveryPhotocatalysisPhotodecarboxylase

Identifiers

PMID39314172
PMCPMC11664916

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Registered trials

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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.