Evidence map›Paper›PMID 32112625›Full record

ArticleMicrobiologyOpen2020

A novel way to synthesize pantothenate in bacteria involves β-alanine synthase present in uracil degradation pathway.

Mariana López-Sámano, Luis Fernando Lozano-Aguirre Beltrán, Rosina Sánchez-Thomas, Araceli Dávalos, Tomás Villaseñor, Jorge Donato García-García, Alejandro García-de Los Santos

Open access · goldAbstract read
In one paragraph

Article in MicrobiologyOpen, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 26 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

7 authors at 1 institution in 1 country.

Mariana López-SámanoPrograma de Ingeniería Genómica, Centro de Ciencias Genómicas, Universidad Nacional Autonoma de México, Cuernavaca, Morelos, México.
Luis Fernando Lozano-Aguirre BeltránPrograma de Ingeniería Genómica, Centro de Ciencias Genómicas, Universidad Nacional Autonoma de México, Cuernavaca, Morelos, México.
Rosina Sánchez-ThomasDepartamento de Bioquímica, Instituto Nacional de Cardiología "Ignacio Chávez", Tlalpan, México.
Araceli DávalosPrograma de Ingeniería Genómica, Centro de Ciencias Genómicas, Universidad Nacional Autonoma de México, Cuernavaca, Morelos, México.
Tomás VillaseñorDepartamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, UNAM, Cuernavaca, México.
Jorge Donato García-GarcíaDepartamento de Bioquímica, Instituto Nacional de Cardiología "Ignacio Chávez", Tlalpan, México.
Alejandro García-de Los SantosPrograma de Ingeniería Genómica, Centro de Ciencias Genómicas, Universidad Nacional Autonoma de México, Cuernavaca, Morelos, México.ORCID 0000-0002-3387-9280
Universidad Nacional Autónoma de México · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pantothenate is an indispensable vitamin precursor of the synthesis of coenzyme A (CoA), a key metabolite required in over 100 metabolic reactions. β-Alanine (β-ala) is an indispensable component of pantothenate. Due to the metabolic relevance of this pathway, we assumed that orthologous genes for ß-alanine synthesis would be present in the genomes of bacteria, archaea, and eukaryotes. However, comparative genomic studies revealed that orthologous gene replacement and loss of synteny occur at high frequency in panD genes. We have previously reported the atypical plasmid-encoded location of the pantothenate pathway genes panC and panB (two copies) in R. etli CFN42. This study also revealed the unexpected absence of a panD gene encoding the aspartate decarboxylase enzyme (ADC), required for the synthesis of β-ala. The aim of this study was to identify the source of β-alanine in Rhizobium etli CFN42. In this study, we present a bioinformatic analysis and an experimental validation demonstrating that the source of β-ala in this R. etli comes from β-alanine synthase, the last enzyme of the uracil degradation pathway.

Indexed as

AgrobacteriumAmidohydrolasesbeta-AlanineCarboxy-LyasesEscherichia coli K12Escherichia coli ProteinsPantothenic AcidRhizobiumUracilAmidohydrolasesaspartate 4-decarboxylasebeta-Alaninebeta-ureidopropionaseCarboxy-LyasesEscherichia coli ProteinsPanD protein, E coliPantothenic AcidUracilCoAcomparative genomicspantothenateuracil degradationvitaminβ-alanine

Identifiers

PMID32112625
PMCPMC7142369
OpenAlexW3008408940

What OpenQuestion holds

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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.