Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism

Metabolism of the mammalian proteinogenic sulfur amino acids methionine and cysteine includes the methionine cycle and reverse transsulfuration pathway, establishing many connections with other important metabolic routes. The main source of these amino acids is the diet, which also provides B vitami...

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Autor: Pajares, María Ángeles
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2025
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/385723
Acceso en línea:http://hdl.handle.net/10261/385723
Access Level:acceso abierto
Palabra clave:Methionine cycle
S-adenosylmethionine
Homocysteine
Posttranslational modification
Transsulfuration
Redox regulation
Oligomerization state
Subcellular localization
Phosphorylation
Acetylation
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spelling Posttranslational Regulation of Mammalian Sulfur Amino Acid MetabolismPajares, María ÁngelesMethionine cycleS-adenosylmethionineHomocysteinePosttranslational modificationTranssulfurationRedox regulationOligomerization stateSubcellular localizationPhosphorylationAcetylationMetabolism of the mammalian proteinogenic sulfur amino acids methionine and cysteine includes the methionine cycle and reverse transsulfuration pathway, establishing many connections with other important metabolic routes. The main source of these amino acids is the diet, which also provides B vitamins required as cofactors for several enzymes of the metabolism of these amino acids. While methionine is considered an essential amino acid, cysteine can be produced from methionine in a series of reactions that also generate homocysteine, a non-proteinogenic amino acid linking reverse transsulfuration with the methionine and folate cycles. These pathways produce key metabolites that participate in synthesizing a large variety of compounds and important regulatory processes (e.g., epigenetic methylations). The impairment of sulfur amino acid metabolism manifests in many pathological processes, mostly correlated with oxidative stress and alterations in glutathione levels that also depend on this part of the cellular metabolism. This review analyzes the current knowledge on the posttranslational regulation of mammalian sulfur amino acid metabolism, highlighting the large number of modification sites reported through high-throughput studies and the surprisingly limited knowledge of their functional impact.This research was funded by the Instituto de Salud Carlos III ERDF (RETIC RIRAAF R16/0006/0021).Peer reviewedMultidisciplinary Digital Publishing InstituteInstituto de Salud Carlos IIIPajares, María Ángeles [0000-0002-4714-9051]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2025202520252025info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/385723reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttps://doi.org/10.3390/ijms26062488Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3857232026-05-22T06:33:51Z
dc.title.none.fl_str_mv Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism
title Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism
spellingShingle Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism
Pajares, María Ángeles
Methionine cycle
S-adenosylmethionine
Homocysteine
Posttranslational modification
Transsulfuration
Redox regulation
Oligomerization state
Subcellular localization
Phosphorylation
Acetylation
title_short Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism
title_full Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism
title_fullStr Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism
title_full_unstemmed Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism
title_sort Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism
dc.creator.none.fl_str_mv Pajares, María Ángeles
author Pajares, María Ángeles
author_facet Pajares, María Ángeles
author_role author
dc.contributor.none.fl_str_mv Instituto de Salud Carlos III
Pajares, María Ángeles [0000-0002-4714-9051]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Methionine cycle
S-adenosylmethionine
Homocysteine
Posttranslational modification
Transsulfuration
Redox regulation
Oligomerization state
Subcellular localization
Phosphorylation
Acetylation
topic Methionine cycle
S-adenosylmethionine
Homocysteine
Posttranslational modification
Transsulfuration
Redox regulation
Oligomerization state
Subcellular localization
Phosphorylation
Acetylation
description Metabolism of the mammalian proteinogenic sulfur amino acids methionine and cysteine includes the methionine cycle and reverse transsulfuration pathway, establishing many connections with other important metabolic routes. The main source of these amino acids is the diet, which also provides B vitamins required as cofactors for several enzymes of the metabolism of these amino acids. While methionine is considered an essential amino acid, cysteine can be produced from methionine in a series of reactions that also generate homocysteine, a non-proteinogenic amino acid linking reverse transsulfuration with the methionine and folate cycles. These pathways produce key metabolites that participate in synthesizing a large variety of compounds and important regulatory processes (e.g., epigenetic methylations). The impairment of sulfur amino acid metabolism manifests in many pathological processes, mostly correlated with oxidative stress and alterations in glutathione levels that also depend on this part of the cellular metabolism. This review analyzes the current knowledge on the posttranslational regulation of mammalian sulfur amino acid metabolism, highlighting the large number of modification sites reported through high-throughput studies and the surprisingly limited knowledge of their functional impact.
publishDate 2025
dc.date.none.fl_str_mv 2025
2025
2025
2025
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/385723
url http://hdl.handle.net/10261/385723
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv https://doi.org/10.3390/ijms26062488
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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