The Lp_3561 and Lp_3562 enzymes support a functional divergence process in the lipase/esterase toolkit from Lactobacillus plantarum

dc.contributor.authorEsteban-Torres, María
dc.contributor.authorReverón, Inés
dc.contributor.authorSantamaría, Laura
dc.contributor.authorMancheño, José M.
dc.contributor.authorde las Rivas, Blanca
dc.contributor.authorMuñoz, Rosario
dc.contributor.funderMinisterio de Economía y Competitividad
dc.contributor.funderInstituto Nacional de Investigación y Tecnología Agraria y Alimentaria
dc.date.accessioned2017-06-20T11:39:45Z
dc.date.available2017-06-20T11:39:45Z
dc.date.issued2016-07-19
dc.description.abstractLactobacillus plantarum species is a good source of esterases since both lipolytic and esterase activities have been described for strains of this species. No fundamental biochemical difference exists among esterases and lipases since both share a common catalytic mechanism. L. plantarum WCFS1 possesses a protein, Lp_3561, which is 44% identical to a previously described lipase, Lp_3562. In contrast to Lp_3562, Lp_3561 was unable to degrade esters possessing a chain length higher than C4 and the triglyceride tributyrin. As in other L. plantarum esterases, the electrostatic potential surface around the active site in Lp_3561 is predicted to be basic, whereas it is essentially neutral in the Lp_3562 lipase. The fact that the genes encoding both proteins were located contiguously in the L. plantarum WCFS1 genome, suggests that they originated by tandem duplication, and therefore are paralogs as new functions have arisen during evolution. The presence of the contiguous lp_3561 and lp_3562 genes was studied among L. plantarum strains. They are located in a 8,903 bp DNA fragment that encodes proteins involved in the catabolism of sialic acid and are predicted to increase bacterial adaptability under certain growth conditions.en
dc.description.sponsorshipMinisterio de Economía y Competitividad(AGL2014-52911R; AGL2011-22745); Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (RM2012-00004).en
dc.description.statusPeer revieweden
dc.description.versionPublished Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.articleid1118
dc.identifier.citationEsteban-Torres, M., Reverón, I., Santamaría, L., Mancheño, J. M., de las Rivas, B. and Muñoz, R. (2016) 'The Lp_3561 and Lp_3562 enzymes support a functional divergence process in the lipase/esterase toolkit from Lactobacillus plantarum', Frontiers in Microbiology, 7,1118 (10pp). doi: 10.3389/fmicb.2016.01118en
dc.identifier.doi10.3389/fmicb.2016.01118
dc.identifier.endpage10
dc.identifier.issn1664-302X
dc.identifier.journaltitleFrontiers in Microbiologyen
dc.identifier.startpage1
dc.identifier.urihttps://hdl.handle.net/10468/4111
dc.identifier.volume7
dc.language.isoenen
dc.publisherFrontiers Mediaen
dc.relation.urihttp://journal.frontiersin.org/article/10.3389/fmicb.2016.01118/full
dc.rights© 2016, Esteban-Torres, Reverón, Santamaría, Mancheño, de las Rivas and Muñoz. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these termsen
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en
dc.subjectEsteraseen
dc.subjectLipaseen
dc.subjectElectrostatic potential surfaceen
dc.subjectTandem duplicationen
dc.subjectParalog genesen
dc.subjectLactic acid bacteriaen
dc.subjectGenomic islanden
dc.titleThe Lp_3561 and Lp_3562 enzymes support a functional divergence process in the lipase/esterase toolkit from Lactobacillus plantarumen
dc.typeArticle (peer-reviewed)en
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