The protein family of pyruvate:quinone oxidoreductases

Detalhes bibliográficos
Autor(a) principal: Sousa, Filipe M.
Data de Publicação: 2023
Outros Autores: Fernandes, Bárbara, Pereira, Manuela M.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/158655
Resumo: Funding Information: FMS is recipient of fellowship by Fundação para a Ciência e a Tecnologia ( PD/BD/128213/2016 , within the scope of the PhD program Molecular Biosciences PD/00133/2012 ). The work was funded by Fundação para a Ciência e a Tecnologia ( PTDC/BIA-BQM/2599/2021 ). The project was supported by UIDB/04046/2020 and UIDP/04046/2020 Centre grants from FCT , Portugal (to BioISI), by LISBOA-01-0145-FEDER-007660 co-funded by FEDER through COMPETE2020-POCI. Publisher Copyright: © 2023 The Author(s)
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spelling The protein family of pyruvate:quinone oxidoreductasesAmino acid sequence conservation and taxonomic distributionAmino-acid residue conservationFlavoproteinsMonotopic quinone reductasesPyruvate metabolismRespiratory chainTaxonomic profileThiamine pyrophosphateBiophysicsBiochemistryCell BiologyFunding Information: FMS is recipient of fellowship by Fundação para a Ciência e a Tecnologia ( PD/BD/128213/2016 , within the scope of the PhD program Molecular Biosciences PD/00133/2012 ). The work was funded by Fundação para a Ciência e a Tecnologia ( PTDC/BIA-BQM/2599/2021 ). The project was supported by UIDB/04046/2020 and UIDP/04046/2020 Centre grants from FCT , Portugal (to BioISI), by LISBOA-01-0145-FEDER-007660 co-funded by FEDER through COMPETE2020-POCI. Publisher Copyright: © 2023 The Author(s)Pyruvate:quinone oxidoreductases (PQOs) catalyse the oxidative decarboxylation of pyruvate to acetate and concomitant reduction of quinone to quinol with the release of CO2. They are thiamine pyrophosphate (TPP) and flavin-adenine dinucleotide (FAD) containing enzymes, which interact with the membrane in a monotopic way. PQOs are considered as part of alternatives to most recognized pyruvate catabolizing pathways, and little is known about their taxonomic distribution and structural/functional relationship. In this bioinformatics work we tackled these gaps in PQO knowledge. We used the KEGG database to identify PQO coding genes, performed a multiple sequence analysis which allowed us to study the amino acid conservation on these enzymes, and looked at their possible cellular function. We observed that PQOS are enzymes exclusively present in prokaryotes with most of the sequences identified in bacteria. Regarding the amino acid sequence conservation, we found that 75 amino acid residues (out of 570, on average) have a conservation over 90 %, and that the most conserved regions in the protein are observed around the TPP and FAD binding sites. We systematized the presence of conserved features involved in Mg2+, TPP and FAD binding, as well as residues directly linked to the catalytic mechanism. We also established the presence of a new motif named “HEH lock”, possibly involved in the dimerization process. The results here obtained for the PQO protein family contribute to a better understanding of the biochemistry of these respiratory enzymes.Instituto de Tecnologia Química e Biológica António Xavier (ITQB)RUNSousa, Filipe M.Fernandes, BárbaraPereira, Manuela M.2023-10-03T22:19:15Z2023-04-012023-04-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/158655eng0005-2728PURE: 72690890https://doi.org/10.1016/j.bbabio.2023.148958info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T05:41:12Zoai:run.unl.pt:10362/158655Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:57:15.305595Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv The protein family of pyruvate:quinone oxidoreductases
Amino acid sequence conservation and taxonomic distribution
title The protein family of pyruvate:quinone oxidoreductases
spellingShingle The protein family of pyruvate:quinone oxidoreductases
Sousa, Filipe M.
Amino-acid residue conservation
Flavoproteins
Monotopic quinone reductases
Pyruvate metabolism
Respiratory chain
Taxonomic profile
Thiamine pyrophosphate
Biophysics
Biochemistry
Cell Biology
title_short The protein family of pyruvate:quinone oxidoreductases
title_full The protein family of pyruvate:quinone oxidoreductases
title_fullStr The protein family of pyruvate:quinone oxidoreductases
title_full_unstemmed The protein family of pyruvate:quinone oxidoreductases
title_sort The protein family of pyruvate:quinone oxidoreductases
author Sousa, Filipe M.
author_facet Sousa, Filipe M.
Fernandes, Bárbara
Pereira, Manuela M.
author_role author
author2 Fernandes, Bárbara
Pereira, Manuela M.
author2_role author
author
dc.contributor.none.fl_str_mv Instituto de Tecnologia Química e Biológica António Xavier (ITQB)
RUN
dc.contributor.author.fl_str_mv Sousa, Filipe M.
Fernandes, Bárbara
Pereira, Manuela M.
dc.subject.por.fl_str_mv Amino-acid residue conservation
Flavoproteins
Monotopic quinone reductases
Pyruvate metabolism
Respiratory chain
Taxonomic profile
Thiamine pyrophosphate
Biophysics
Biochemistry
Cell Biology
topic Amino-acid residue conservation
Flavoproteins
Monotopic quinone reductases
Pyruvate metabolism
Respiratory chain
Taxonomic profile
Thiamine pyrophosphate
Biophysics
Biochemistry
Cell Biology
description Funding Information: FMS is recipient of fellowship by Fundação para a Ciência e a Tecnologia ( PD/BD/128213/2016 , within the scope of the PhD program Molecular Biosciences PD/00133/2012 ). The work was funded by Fundação para a Ciência e a Tecnologia ( PTDC/BIA-BQM/2599/2021 ). The project was supported by UIDB/04046/2020 and UIDP/04046/2020 Centre grants from FCT , Portugal (to BioISI), by LISBOA-01-0145-FEDER-007660 co-funded by FEDER through COMPETE2020-POCI. Publisher Copyright: © 2023 The Author(s)
publishDate 2023
dc.date.none.fl_str_mv 2023-10-03T22:19:15Z
2023-04-01
2023-04-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10362/158655
url http://hdl.handle.net/10362/158655
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0005-2728
PURE: 72690890
https://doi.org/10.1016/j.bbabio.2023.148958
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
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