Evidence map›Paper›PMID 30426381›Full record

ArticleMolecular biology reports2019

Substrate and inhibitor selectivity, and biological activity of an epoxide hydrolase from Trichoderma reesei.

Gabriel S de Oliveira, Patricia P Adriani, Hao Wu, Christophe Morisseau, Bruce D Hammock, Felipe S Chambergo

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular biology reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 46% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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 2 institutions in 2 countries.

Gabriel S de OliveiraEscola de Artes, Ciências e Humanidades, Universidade de São Paulo, 1000 Av. Arlindo Bettio, Ermelino Matarazzo, CEP: 03828-000, São Paulo, Brazil.
Patricia P AdrianiEscola de Artes, Ciências e Humanidades, Universidade de São Paulo, 1000 Av. Arlindo Bettio, Ermelino Matarazzo, CEP: 03828-000, São Paulo, Brazil.
Hao WuDepartment of Entomology and Nematology, and UC Davis Comprehensive Cancer Center, University of California, One Shields Avenue, Davis, CA, USA.
Christophe MorisseauDepartment of Entomology and Nematology, and UC Davis Comprehensive Cancer Center, University of California, One Shields Avenue, Davis, CA, USA.
Bruce D HammockDepartment of Entomology and Nematology, and UC Davis Comprehensive Cancer Center, University of California, One Shields Avenue, Davis, CA, USA.
Felipe S ChambergoEscola de Artes, Ciências e Humanidades, Universidade de São Paulo, 1000 Av. Arlindo Bettio, Ermelino Matarazzo, CEP: 03828-000, São Paulo, Brazil. fscha@usp.br.ORCID http://orcid.org/0000-0001-7567-0656
UC Davis Comprehensive Cancer CenterUniversidade de São Paulo · BR

Funding

Workshop on Environmental Technology Transfer and EntrepreneurshipP42ES004699 · NIEHS · UNIVERSITY OF CALIFORNIA DAVIS · PI HAMMOCK, BRUCE D · 1987 to 2021
$50.1M
HYDROLYTIC ENZYMES IN THE METABOLISM OF TOXINSR01ES002710 · NIEHS · UNIVERSITY OF CALIFORNIA DAVIS · PI HAMMOCK, BRUCE D · 1985 to 2018
$4.0M
Fundação de Amparo à Pesquisa do Estado de São Paulo 2014/24107-1Fundação de Amparo à Pesquisa do Estado de São Paulo 2017/25705-8National Institute of Environmental Health Sciences NIEHS-R01 ES002710National Institute of Environmental Health Sciences P42 ES 04699NIEHS NIH HHS P42 ES004699NIEHS NIH HHS R01 ES002710
6 · The paper itself

Abstract

Epoxide hydrolases (EHs) are present in all living organisms and catalyze the hydrolysis of epoxides to the corresponding vicinal diols. EH are involved in the metabolism of endogenous and exogenous epoxides, and thus have application in pharmacology and biotechnology. In this work, we describe the substrates and inhibitors selectivity of an epoxide hydrolase recently cloned from the filamentous fungus Trichoderma reesei QM9414 (TrEH). We also studied the TrEH urea-based inhibitors effects in the fungal growth. TrEH showed high activity on radioative and fluorescent surrogate and natural substrates, especially epoxides from docosahexaenoic acid. Using a fluorescent surrogate substrate, potent inhibitors of TrEH were identified. Interestingly, one of the best compounds inhibit up to 60% of T. reesei growth, indicating an endogenous role for TrEH. These data make TrEH very attractive for future studies about fungal metabolism of fatty acids and possible development of novel drugs for human diseases.

Indexed as

CatalysisEpoxide HydrolasesEpoxy CompoundsFatty AcidsHydrolysisTrichodermaEpoxide HydrolasesEpoxy CompoundsFatty AcidsEH inhibitorsEpoxide hydrolaseEpoxy fatty acidsGrowth inhibitory activityTrichoderma reesei

Identifiers

PMID30426381
PMCPMC6426676
OpenAlexW2901556281

What OpenQuestion holds

Textmetadata
LicenceTDM
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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.