Evidence map›Paper›PMID 32581293›Full record

ArticleScientific reports2020

Phylogeny, evolution, and potential ecological relationship of cytochrome CYP52 enzymes in Saccharomycetales yeasts.

Jossue Ortiz-Álvarez, Arturo Becerra-Bracho, Alfonso Méndez-Tenorio, Jazmin Murcia-Garzón, Lourdes Villa-Tanaca, César Hernández-Rodríguez

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

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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 1 country.

Jossue Ortiz-ÁlvarezLaboratorio de Biología Molecular de Bacterias y Levaduras. Departamento de Microbiología, Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Prol. de Carpio y Plan de Ayala s/n. Col. Sto. Tomás, 11340, Ciudad de México, México.
Arturo Becerra-BrachoFacultad de Ciencias, Universidad Nacional Autónoma de México, Apdo. Postal 70-407, Cd. Universitaria, 04510, Ciudad de México, México.
Alfonso Méndez-TenorioDepartamento de Bioquímica, Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Prol. de Carpio y Plan de Ayala s/n. Col. Sto. Tomás, 11340, Ciudad de México, México.
Jazmin Murcia-GarzónDepartamento de Bioquímica, Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Prol. de Carpio y Plan de Ayala s/n. Col. Sto. Tomás, 11340, Ciudad de México, México.
Lourdes Villa-TanacaLaboratorio de Biología Molecular de Bacterias y Levaduras. Departamento de Microbiología, Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Prol. de Carpio y Plan de Ayala s/n. Col. Sto. Tomás, 11340, Ciudad de México, México.
César Hernández-RodríguezLaboratorio de Biología Molecular de Bacterias y Levaduras. Departamento de Microbiología, Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Prol. de Carpio y Plan de Ayala s/n. Col. Sto. Tomás, 11340, Ciudad de México, México. chdez38@hotmail.com.
Instituto Politécnico Nacional · MXUniversidad Nacional Autónoma de México · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytochrome P450s from the CYP52 family participate in the assimilation of alkanes and fatty acids in fungi. In this work, the evolutionary history of a set of orthologous and paralogous CYP52 proteins from Saccharomycetales yeasts was inferred. Further, the phenotypic assimilation profiles were related with the distribution of cytochrome CYP52 members among species. The maximum likelihood phylogeny of CYP52 inferred proteins reveled a frequent ancient and modern duplication and loss events that generated orthologous and paralogous groups. Phylogeny and assimilation profiles of alkanes and fatty acids showed a family expansion in yeast isolated from hydrophobic-rich environments. Docking analysis of deduced ancient CYP52 proteins suggests that the most ancient function was the oxidation of C4-C11 alkanes, while the oxidation of >10 carbon alkanes and fatty acids is a derived character. The ancient CYP52 paralogs displayed partial specialization and promiscuous interaction with hydrophobic substrates. Additionally, functional optimization was not evident. Changes in the interaction of ancient CYP52 with different alkanes and fatty acids could be associated with modifications in spatial orientations of the amino acid residues that comprise the active site. The extended family of CYP52 proteins is likely evolving toward functional specialization, and certain redundancy for substrates is being maintained.

Indexed as

AlkanesCytochrome P-450 Enzyme SystemEvolution, MolecularFatty AcidsFungal ProteinsMolecular Docking SimulationOxidation-ReductionPhylogenySaccharomycetalesSubstrate SpecificityAlkanesCytochrome P-450 Enzyme SystemFatty AcidsFungal Proteins

Identifiers

PMID32581293
PMCPMC7314818
OpenAlexW3037398051

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.