Enzymatic systems of inorganic pyrophosphate bioenergetics in photosynthetic and heterotrophic protists: remmants or metabolic cornerstones?

An increasing body of biochemical and genetic evidence suggests that inorganic pyrophosphate (PPi) plays an important role in protist bioenergetics. In these organisms, two types of inorganic pyrophosphatases [EC 3.6.1.1, namely soluble PPases (sPPases) and proton-translocating PPases (H+-PPases)] t...

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Autores: Losada Villasante, Manuel, Pérez Castiñeira, José Román, Gómez García, Rosario, López Marqués, Rosa Laura, Serrano Delgado, Aurelio
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2001
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/26068
Acceso en línea:http://hdl.handle.net/11441/26068
https://doi.org/10.1007/s10123-001-0028-x
Access Level:acceso abierto
Palabra clave:Inorganic pyrophosphate
Soluble inorganic pyrophophatase
Proton-translocating pyrophosphatase
Photosynthetic protists
Parasitic protists
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spelling Enzymatic systems of inorganic pyrophosphate bioenergetics in photosynthetic and heterotrophic protists: remmants or metabolic cornerstones?Losada Villasante, ManuelPérez Castiñeira, José RománGómez García, RosarioLópez Marqués, Rosa LauraSerrano Delgado, AurelioInorganic pyrophosphateSoluble inorganic pyrophophataseProton-translocating pyrophosphatasePhotosynthetic protistsParasitic protistsAn increasing body of biochemical and genetic evidence suggests that inorganic pyrophosphate (PPi) plays an important role in protist bioenergetics. In these organisms, two types of inorganic pyrophosphatases [EC 3.6.1.1, namely soluble PPases (sPPases) and proton-translocating PPases (H+-PPases)] that hydrolyse the PPi generated by cell anabolism, thereby replenishing the orthophosphate pool needed for phosphorylation reactions, are present in different cellular compartments. Photosynthetic and heterotrophic protists possess sPPases located in cellular organelles (plastids and mitochondria), where many anabolic and biosynthetic reactions take place, in addition to H+-PPases, which are integral membrane proteins of the vacuolysosomal membranes and use the chemical energy of PPi to generate an electrochemical proton gradient useful in cell bioenergetics. This last category of proton pumps was considered to be restricted to higher plants and some primitive photosynthetic bacteria, but it has been found recently in many protists (microalgae and protozoa) and bacteria, thus indicating that H+-PPases are much more widespread than previously thought. No cytosolic sPPase (in bacteria, fungi and animal cells) has been shown to occur in these lower eukaryotes. The widespread occurrence of these key enzymes of PPi metabolism among evolutionarily divergent protists strongly supports the ancestral character of the bioenergetics based on this simple energy-rich compound, which may play an important role in survival under different biotic and abiotic stress conditions.SpringerBioquímica Vegetal y Biología Molecular2001info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttp://hdl.handle.net/11441/26068https://doi.org/10.1007/s10123-001-0028-xreponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésInternational microbiology, 4 (3), 135-142.10.1007/s10123-001-0028-xinfo:eu-repo/semantics/openAccessoai:idus.us.es:11441/260682026-06-17T12:51:07Z
dc.title.none.fl_str_mv Enzymatic systems of inorganic pyrophosphate bioenergetics in photosynthetic and heterotrophic protists: remmants or metabolic cornerstones?
title Enzymatic systems of inorganic pyrophosphate bioenergetics in photosynthetic and heterotrophic protists: remmants or metabolic cornerstones?
spellingShingle Enzymatic systems of inorganic pyrophosphate bioenergetics in photosynthetic and heterotrophic protists: remmants or metabolic cornerstones?
Losada Villasante, Manuel
Inorganic pyrophosphate
Soluble inorganic pyrophophatase
Proton-translocating pyrophosphatase
Photosynthetic protists
Parasitic protists
title_short Enzymatic systems of inorganic pyrophosphate bioenergetics in photosynthetic and heterotrophic protists: remmants or metabolic cornerstones?
title_full Enzymatic systems of inorganic pyrophosphate bioenergetics in photosynthetic and heterotrophic protists: remmants or metabolic cornerstones?
title_fullStr Enzymatic systems of inorganic pyrophosphate bioenergetics in photosynthetic and heterotrophic protists: remmants or metabolic cornerstones?
title_full_unstemmed Enzymatic systems of inorganic pyrophosphate bioenergetics in photosynthetic and heterotrophic protists: remmants or metabolic cornerstones?
title_sort Enzymatic systems of inorganic pyrophosphate bioenergetics in photosynthetic and heterotrophic protists: remmants or metabolic cornerstones?
dc.creator.none.fl_str_mv Losada Villasante, Manuel
Pérez Castiñeira, José Román
Gómez García, Rosario
López Marqués, Rosa Laura
Serrano Delgado, Aurelio
author Losada Villasante, Manuel
author_facet Losada Villasante, Manuel
Pérez Castiñeira, José Román
Gómez García, Rosario
López Marqués, Rosa Laura
Serrano Delgado, Aurelio
author_role author
author2 Pérez Castiñeira, José Román
Gómez García, Rosario
López Marqués, Rosa Laura
Serrano Delgado, Aurelio
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Bioquímica Vegetal y Biología Molecular
dc.subject.none.fl_str_mv Inorganic pyrophosphate
Soluble inorganic pyrophophatase
Proton-translocating pyrophosphatase
Photosynthetic protists
Parasitic protists
topic Inorganic pyrophosphate
Soluble inorganic pyrophophatase
Proton-translocating pyrophosphatase
Photosynthetic protists
Parasitic protists
description An increasing body of biochemical and genetic evidence suggests that inorganic pyrophosphate (PPi) plays an important role in protist bioenergetics. In these organisms, two types of inorganic pyrophosphatases [EC 3.6.1.1, namely soluble PPases (sPPases) and proton-translocating PPases (H+-PPases)] that hydrolyse the PPi generated by cell anabolism, thereby replenishing the orthophosphate pool needed for phosphorylation reactions, are present in different cellular compartments. Photosynthetic and heterotrophic protists possess sPPases located in cellular organelles (plastids and mitochondria), where many anabolic and biosynthetic reactions take place, in addition to H+-PPases, which are integral membrane proteins of the vacuolysosomal membranes and use the chemical energy of PPi to generate an electrochemical proton gradient useful in cell bioenergetics. This last category of proton pumps was considered to be restricted to higher plants and some primitive photosynthetic bacteria, but it has been found recently in many protists (microalgae and protozoa) and bacteria, thus indicating that H+-PPases are much more widespread than previously thought. No cytosolic sPPase (in bacteria, fungi and animal cells) has been shown to occur in these lower eukaryotes. The widespread occurrence of these key enzymes of PPi metabolism among evolutionarily divergent protists strongly supports the ancestral character of the bioenergetics based on this simple energy-rich compound, which may play an important role in survival under different biotic and abiotic stress conditions.
publishDate 2001
dc.date.none.fl_str_mv 2001
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11441/26068
https://doi.org/10.1007/s10123-001-0028-x
url http://hdl.handle.net/11441/26068
https://doi.org/10.1007/s10123-001-0028-x
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv International microbiology, 4 (3), 135-142.
10.1007/s10123-001-0028-x
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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