Evidence map›Paper›PMID 42157621›Full record

ArticleThe FEBS journal2026

Caffeylpyruvate hydrolase from the bioluminescent fungus Neonothopanus gardneri is the key recycling enzyme in the fungal bioluminescence pathway.

Caio K Zamuner, Douglas M M Soares, Bianca B Nóbrega, Etelvino J H Bechara, Zinaida M Kaskova, Alexander S Mishin, Karen S Sarkisyan, Ilia V Yampolsky, Cassius V Stevani

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Article in The FEBS journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

9 authors.

Caio K ZamunerDepartamento de Química Fundamental, Instituto de Química, Universidade de São Paulo, Brazil.
Douglas M M SoaresDepartment of Bioprocess Engineering and Biotechnology, School of Pharmaceutical Sciences, São Paulo State University, Araraquara, Brazil.
Bianca B NóbregaDepartamento de Química Fundamental, Instituto de Química, Universidade de São Paulo, Brazil.
Etelvino J H BecharaDepartamento de Química Fundamental, Instituto de Química, Universidade de São Paulo, Brazil.
Zinaida M KaskovaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Alexander S MishinShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.ORCID https://orcid.org/0000-0002-4935-7030
Karen S SarkisyanSynthetic Biology Group, MRC Laboratory of Medical Sciences, London, UK.
Ilia V YampolskyShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.ORCID https://orcid.org/0000-0003-2558-2476
Cassius V StevaniDepartamento de Química Fundamental, Instituto de Química, Universidade de São Paulo, Brazil.ORCID https://orcid.org/0000-0002-7209-7476

Funding

Conselho Nacional de Desenvolvimento Científico e Tecnológico 303393/2024-6Conselho Nacional de Desenvolvimento Científico e Tecnológico 306460/2016-5Fundação de Amparo à Pesquisa do Estado de São Paulo 2017/22501-2Fundação de Amparo à Pesquisa do Estado de São Paulo 2019/12605-0Fundação de Amparo à Pesquisa do Estado de São Paulo 2019/21782-3Fundação de Amparo à Pesquisa do Estado de São Paulo 2020/16000-3Fundação de Amparo à Pesquisa do Estado de São Paulo 2022/14964-0Medical Research Council UKRI MC-A658-5QEA0Russian Science Foundation 25-14-00349Russian Science Foundation 25-76-30006
6 · The paper itself

Abstract

Recent studies uncovered the fungal bioluminescence pathway (FBP), a biosynthetic signaling axis to which caffeic acid is central. A key step, the hydrolysis of oxyluciferin into caffeic and pyruvic acids, was previously observed only in crude extracts, with pyruvate formation uncertain. Using gene homology, we identified and cloned cph from Neonothopanus gardneri, encoding a predicted fumarylacetoacetate hydrolase (FAH)-family enzyme, named ngarCPH. We successfully expressed and purified ngarCPH and demonstrated its catalytic activity on oxyluciferin, confirming formation of both products. Kinetic characterization revealed the optimal temperature and pH, while structural modeling and multiple sequence alignment indicate characteristics similar to those of FAH enzymes. This work not only expands the knowledge of the function of enzymes from the FAH superfamily but also confirms a complete, self-sustained bioluminescence cycle in fungi. Our findings support the future development of autonomous bioluminescent systems in heterologous hosts.

Indexed as

BasidiomycotaFungal ProteinsHydrolasesAmino Acid SequenceCaffeic AcidsCloning, MolecularHydrogen-Ion ConcentrationKineticsLuminescenceModels, MolecularCaffeic AcidsfumarylacetoacetaseFungal ProteinsHydrolasesbasidiomycetefumarylacetoacetate hydrolase superfamilyfungal bioluminescenceretro aldol condensation

Identifiers

PMID42157621
PMCPMC13669639

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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.