Cargando…

Identification of functional signatures in the metabolism of the three cellular domains of life

In order to identify common and specific enzymatic activities associated with the metabolism of the three cellular domains of life, the conservation and variations between the enzyme contents of Bacteria, Archaea, and Eukarya organisms were evaluated. To this end, the content of enzymes belonging to...

Descripción completa

Detalles Bibliográficos
Autores principales: Escobar-Turriza, Pedro, Hernandez-Guerrero, Rafael, Poot-Hernández, Augusto Cesar, Rodríguez-Vázquez, Katya, Ramírez-Prado, Jorge, Pérez-Rueda, Ernesto
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6538242/
https://www.ncbi.nlm.nih.gov/pubmed/31136618
http://dx.doi.org/10.1371/journal.pone.0217083
_version_ 1783422164576239616
author Escobar-Turriza, Pedro
Hernandez-Guerrero, Rafael
Poot-Hernández, Augusto Cesar
Rodríguez-Vázquez, Katya
Ramírez-Prado, Jorge
Pérez-Rueda, Ernesto
author_facet Escobar-Turriza, Pedro
Hernandez-Guerrero, Rafael
Poot-Hernández, Augusto Cesar
Rodríguez-Vázquez, Katya
Ramírez-Prado, Jorge
Pérez-Rueda, Ernesto
author_sort Escobar-Turriza, Pedro
collection PubMed
description In order to identify common and specific enzymatic activities associated with the metabolism of the three cellular domains of life, the conservation and variations between the enzyme contents of Bacteria, Archaea, and Eukarya organisms were evaluated. To this end, the content of enzymes belonging to a particular pathway and their abundance and distribution in 1507 organisms that have been annotated and deposited in the KEGG database were assessed. In addition, we evaluated the consecutive enzymatic reaction pairs obtained from metabolic pathway reactions and transformed into sequences of enzymatic reactions, with catalytic activities encoded in the Enzyme Commission numbers, which are linked by a substrate. Both analyses are complementary: the first considers individual reactions associated with each organism and metabolic map, and the second evaluates the functional associations between pairs of consecutive reactions. From these comparisons, we found a set of five enzymatic reactions that were widely distributed in all the organisms and considered here as universal to Bacteria, Archaea, and Eukarya; whereas 132 pairs out of 3151 reactions were identified as significant, only 5 of them were found to be widely distributed in all the taxonomic divisions. However, these universal reactions are not widely distributed along the metabolic maps, suggesting their dispensability to all metabolic processes. Finally, we found that universal reactions are also associated with ancestral domains, such as those related to phosphorus-containing groups with a phosphate group as acceptor or those related to the ribulose-phosphate binding barrel, triosephosphate isomerase, and D-ribose-5-phosphate isomerase (RpiA) lid domain, among others. Therefore, we consider that this analysis provides clues about the functional constraints associated with the repertoire of enzymatic functions per organism.
format Online
Article
Text
id pubmed-6538242
institution National Center for Biotechnology Information
language English
publishDate 2019
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-65382422019-06-05 Identification of functional signatures in the metabolism of the three cellular domains of life Escobar-Turriza, Pedro Hernandez-Guerrero, Rafael Poot-Hernández, Augusto Cesar Rodríguez-Vázquez, Katya Ramírez-Prado, Jorge Pérez-Rueda, Ernesto PLoS One Research Article In order to identify common and specific enzymatic activities associated with the metabolism of the three cellular domains of life, the conservation and variations between the enzyme contents of Bacteria, Archaea, and Eukarya organisms were evaluated. To this end, the content of enzymes belonging to a particular pathway and their abundance and distribution in 1507 organisms that have been annotated and deposited in the KEGG database were assessed. In addition, we evaluated the consecutive enzymatic reaction pairs obtained from metabolic pathway reactions and transformed into sequences of enzymatic reactions, with catalytic activities encoded in the Enzyme Commission numbers, which are linked by a substrate. Both analyses are complementary: the first considers individual reactions associated with each organism and metabolic map, and the second evaluates the functional associations between pairs of consecutive reactions. From these comparisons, we found a set of five enzymatic reactions that were widely distributed in all the organisms and considered here as universal to Bacteria, Archaea, and Eukarya; whereas 132 pairs out of 3151 reactions were identified as significant, only 5 of them were found to be widely distributed in all the taxonomic divisions. However, these universal reactions are not widely distributed along the metabolic maps, suggesting their dispensability to all metabolic processes. Finally, we found that universal reactions are also associated with ancestral domains, such as those related to phosphorus-containing groups with a phosphate group as acceptor or those related to the ribulose-phosphate binding barrel, triosephosphate isomerase, and D-ribose-5-phosphate isomerase (RpiA) lid domain, among others. Therefore, we consider that this analysis provides clues about the functional constraints associated with the repertoire of enzymatic functions per organism. Public Library of Science 2019-05-28 /pmc/articles/PMC6538242/ /pubmed/31136618 http://dx.doi.org/10.1371/journal.pone.0217083 Text en © 2019 Escobar-Turriza et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Escobar-Turriza, Pedro
Hernandez-Guerrero, Rafael
Poot-Hernández, Augusto Cesar
Rodríguez-Vázquez, Katya
Ramírez-Prado, Jorge
Pérez-Rueda, Ernesto
Identification of functional signatures in the metabolism of the three cellular domains of life
title Identification of functional signatures in the metabolism of the three cellular domains of life
title_full Identification of functional signatures in the metabolism of the three cellular domains of life
title_fullStr Identification of functional signatures in the metabolism of the three cellular domains of life
title_full_unstemmed Identification of functional signatures in the metabolism of the three cellular domains of life
title_short Identification of functional signatures in the metabolism of the three cellular domains of life
title_sort identification of functional signatures in the metabolism of the three cellular domains of life
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6538242/
https://www.ncbi.nlm.nih.gov/pubmed/31136618
http://dx.doi.org/10.1371/journal.pone.0217083
work_keys_str_mv AT escobarturrizapedro identificationoffunctionalsignaturesinthemetabolismofthethreecellulardomainsoflife
AT hernandezguerrerorafael identificationoffunctionalsignaturesinthemetabolismofthethreecellulardomainsoflife
AT poothernandezaugustocesar identificationoffunctionalsignaturesinthemetabolismofthethreecellulardomainsoflife
AT rodriguezvazquezkatya identificationoffunctionalsignaturesinthemetabolismofthethreecellulardomainsoflife
AT ramirezpradojorge identificationoffunctionalsignaturesinthemetabolismofthethreecellulardomainsoflife
AT perezruedaernesto identificationoffunctionalsignaturesinthemetabolismofthethreecellulardomainsoflife