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The protein family of pyruvate:quinone oxidoreductases

2023-04-01Artigo científico Acesso aberto
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dc.contributor.authorSousa, Filipe M.
dc.contributor.authorFernandes, Bárbara
dc.contributor.authorPereira, Manuela M.
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.pblElsevier BV
dc.date.accessioned2023-10-03T22:19:15Z
dc.date.available2023-10-03T22:19:15Z
dc.date.issued2023-04-01
dc.descriptionFunding 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)
dc.description.abstractPyruvate: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.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent8709489
dc.identifier.doi10.1016/j.bbabio.2023.148958
dc.identifier.issn0005-2728
dc.identifier.otherPURE: 72690890
dc.identifier.otherPURE UUID: 2fbfb657-7ff0-4a50-81e1-bc0ed54cf609
dc.identifier.otherScopus: 85147579935
dc.identifier.otherPubMed: 36758662
dc.identifier.urihttp://hdl.handle.net/10362/158655
dc.identifier.urlhttps://www.scopus.com/pages/publications/85147579935
dc.language.isoeng
dc.peerreviewedyes
dc.subjectAmino-acid residue conservation
dc.subjectFlavoproteins
dc.subjectMonotopic quinone reductases
dc.subjectPyruvate metabolism
dc.subjectRespiratory chain
dc.subjectTaxonomic profile
dc.subjectThiamine pyrophosphate
dc.subjectBiophysics
dc.subjectBiochemistry
dc.subjectCell Biology
dc.titleThe protein family of pyruvate:quinone oxidoreductasesen
dc.title.subtitleAmino acid sequence conservation and taxonomic distributionen
dc.typejournal article
degois.publication.issue2
degois.publication.titleBiochimica et Biophysica Acta - Bioenergetics
degois.publication.volume1864
dspace.entity.typePublication
rcaap.rightsopenAccess

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