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Anaerobic sulfatase maturase AslB from Escherichia coli activates human recombinant iduronate-2-sulfate sulfatase (IDS) and N-acetylgalactosamine-6-sulfate sulfatase (GALNS)

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dc.creatorAlméciga-Díaz C.J.spa
dc.creatorTolosa-Díaz A.D.spa
dc.creatorPimentel L.N.spa
dc.creatorBonilla Y.A.spa
dc.creatorRodríguez-López A.spa
dc.creatorEspejo-Mojica A.J.spa
dc.creatorPatiño J.D.spa
dc.creatorSánchez O.F.spa
dc.creatorGonzalez-Santos J.spa
dc.date.accessioned2020-05-26T00:09:00Z
dc.date.available2020-05-26T00:09:00Z
dc.date.created2017spa
dc.description.abstractMaturation of type I sulfatases requires the conversion of the cysteine (Cys) or serine (Ser) present in the active site to formylglycine (FGly). This activation represents a limiting step during the production of recombinant sulfatases in bacteria and eukaryotic hosts. AslB, YdeM and YidF have been proposed to participate in the activation of sulfatases in Escherichia coli. In this study, we combined in-silico and experimental approaches to study the interaction between Escherichia coli BL21(DE3) AslB and human sulfatases, more specifically iduronate-2-sulfate sulfatase (IDS) and N-acetylgalactosamine-6-sulfate sulfatase (GALNS). In-silico results show that AslB has a higher affinity for the residual motif of GALNS (? 9.4 kcal mol? 1), Cys- and Ser-type, than for the one of IDS (? 8.0 kcal mol? 1). However, the distance between the AslB active residue and the target motif favors the interaction with IDS (4.4 Å) more than with GALNS (5.5 Å). Experimental observations supported in-silico results where the co-expression of AslB with GALNS Cys- and Ser-type presented an activity increment of 2.0- and 1.5-fold compared to the control cultures, lacking overexpressed AslB. Similarly, IDS activity was increased in 4.6-fold when co-expressed with AslB. The higher sulfatase activity of AslB-IDS suggests that the distance between the AslB active residue and the motif target is a key parameter for the in-silico search of potential sulfatase activators. In conclusion, our results suggest that AslB is involve in the maturation of heterologous human sulfatases in E. coli BL21(DE3), and that it can have important implications in the production of recombinant sulfatases for therapeutic purposes and research. © 2017 Elsevier B.V.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.gene.2017.08.043
dc.identifier.issn3781119
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/24133
dc.language.isoengspa
dc.publisherElsevier B.V.spa
dc.relation.citationEndPage61
dc.relation.citationStartPage53
dc.relation.citationTitleGene
dc.relation.citationVolumeVol. 634
dc.relation.ispartofGene, ISSN:3781119, Vol.634,(2017); pp. 53-61spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85030621013&doi=10.1016%2fj.gene.2017.08.043&partnerID=40&md5=54cc47edce5953b01cc5fce3d0fcf602spa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.source.instnameinstname:Universidad del Rosariospa
dc.source.reponamereponame:Repositorio Institucional EdocURspa
dc.subject.keywordAnaerobic sulfatase maturase aslbspa
dc.subject.keywordCysteinespa
dc.subject.keywordIduronate 2 sulfatasespa
dc.subject.keywordN acetylgalactosamine 6 sulfatasespa
dc.subject.keywordRecombinant enzymespa
dc.subject.keywordSerinespa
dc.subject.keywordSulfatasespa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordEscherichia coli proteinspa
dc.subject.keywordGALNS proteineng
dc.subject.keywordGlycoproteinspa
dc.subject.keywordIDS proteineng
dc.subject.keywordN acetylgalactosamine 4 sulfatasespa
dc.subject.keywordProtein bindingspa
dc.subject.keywordRecombinant proteinspa
dc.subject.keywordSulfatasespa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordArticlespa
dc.subject.keywordBinding affinityspa
dc.subject.keywordControlled studyspa
dc.subject.keywordEnzyme activationspa
dc.subject.keywordEnzyme active sitespa
dc.subject.keywordEnzyme activityspa
dc.subject.keywordEscherichia colispa
dc.subject.keywordMolecular dockingspa
dc.subject.keywordMolecular dynamicsspa
dc.subject.keywordMolecular modelspa
dc.subject.keywordNonhumanspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProtein expressionspa
dc.subject.keywordProtein motifspa
dc.subject.keywordProtein protein interactionspa
dc.subject.keywordChemistryspa
dc.subject.keywordEnzyme activationspa
dc.subject.keywordEnzymologyspa
dc.subject.keywordEscherichia colispa
dc.subject.keywordHumanspa
dc.subject.keywordMetabolismspa
dc.subject.keywordCatalytic Domainspa
dc.subject.keywordChondroitinsulfatasesspa
dc.subject.keywordCysteinespa
dc.subject.keywordEnzyme Activationspa
dc.subject.keywordEscherichia colispa
dc.subject.keywordEscherichia coli Proteinsspa
dc.subject.keywordGlycoproteinsspa
dc.subject.keywordHumansspa
dc.subject.keywordModelseng
dc.subject.keywordMolecular Docking Simulationspa
dc.subject.keywordMolecular Dynamics Simulationspa
dc.subject.keywordProtein Bindingspa
dc.subject.keywordRecombinant Proteinsspa
dc.subject.keywordSerinespa
dc.subject.keywordSulfatasesspa
dc.subject.keywordAslbspa
dc.subject.keywordFormylglycine-generating enzymesspa
dc.subject.keywordIduronate-2-sulfate sulfatasespa
dc.subject.keywordN-acetylgalactosamine-6-sulfate sulfatasespa
dc.subject.keywordSulfatasesspa
dc.titleAnaerobic sulfatase maturase AslB from Escherichia coli activates human recombinant iduronate-2-sulfate sulfatase (IDS) and N-acetylgalactosamine-6-sulfate sulfatase (GALNS)spa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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