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dc.contributor.authorAcosta, Javierspa
dc.contributor.authorDel Arco, Jonspa
dc.contributor.authorPisabarro, Victorspa
dc.contributor.authorGago, Federicospa
dc.contributor.authorFernández-Lucas, Jesússpa
dc.date.accessioned2020-07-07T19:15:03Z
dc.date.available2020-07-07T19:15:03Z
dc.date.issued2020-06-20
dc.identifier.issn2296-4185spa
dc.identifier.urihttps://hdl.handle.net/11323/6474spa
dc.description.abstractNucleoside-2′-deoxyribosyl-transferases (NDTs) catalyze a transglycosylation reaction consisting of the exchange of the 2′-deoxyribose moiety between a purine and/or pyrimidine nucleoside and a purine and/or pyrimidine base. Because NDTs are highly specific for 2′-deoxyribonucleosides they generally display poor activity on modified C2′ and C3′ nucleosides and this limitation hampers their applicability as biocatalysts for the synthesis of modified nucleosides. We now report the production and purification of a novel NDT from Archaeoglobus veneficus that is endowed with native ribosyltransferase activity and hence it is more properly classified as an N-ribosyltransferase (AvNRT). Biophysical and biochemical characterization revealed that AvNRT is a homotetramer that displays maximum activity at 80°C and pH 6 and shows remarkably high stability at high temperatures (60–80°C). In addition, the activity of AvNRT was found to increase up to 2-fold in 4 M NaCl aqueous solution and to be retained in the presence of several water-miscible organic solvents. For completeness, and as a proof of concept for possible industrial applications, this thermophilic and halotolerant biocatalyst was successfully employed in the synthesis of different purine ribonucleoside analogs.spa
dc.language.isoeng
dc.publisherFrontiers in Bioengineering and Biotechnologyspa
dc.rightsCC0 1.0 Universalspa
dc.rights.urihttp://creativecommons.org/publicdomain/zero/1.0/spa
dc.subjectNucleosidesspa
dc.subjectExtremophilesspa
dc.subjectNucleoside 2′-deoxyribosyltransferasespa
dc.subjectTransglycosylationspa
dc.subjectHomology modelingspa
dc.titleN-Ribosyltransferase From Archaeoglobus veneficus: A Novel Halotolerant and Thermostable Biocatalyst for the Synthesis of Purine Ribonucleoside Analogsspa
dc.typeArtículo de revistaspa
dc.rights.accessrightsinfo:eu-repo/semantics/openAccessspa
dc.identifier.doihttps://doi.org/10.3389/fbioe.2020.00593spa
dc.identifier.instnameCorporación Universidad de la Costaspa
dc.identifier.reponameREDICUC - Repositorio CUCspa
dc.identifier.repourlhttps://repositorio.cuc.edu.co/spa
dc.relation.referencesThomson, J., and Lamont, I. (2019). Nucleoside analogues as antibacterial agents. Front. Microbiol. 10:952. doi: 10.3389/fmicb.2019.00952spa
dc.relation.referencesTrelles, J., Rivero, C. N., Britos, C. J., and Lapponi, M. (2019). “Enzymatic synthesis of nucleic acid derivatives by immobilized cells,” in Enzymatic and Chemical Synthesis of Nucleic Acid Derivatives, eds J. Fernández-Lucas and M. J. Camarasa (Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KgaA), 79–106.spa
dc.relation.referencesVichier-Guerre, S., Dugué, L., Bonhomme, F., and Pochet, S. (2017). An expedient synthesis of flexible nucleosides via a regiocontrolled enzymatic glycosylation of functionalized imidazoles. Org. Biomol. Chem. 15, 8193–8203. doi: 10.1039/c7ob01850aspa
dc.relation.referencesYe, W., Paul, D., Gao, L., Seckute, J., Sangaiah, R., Jayaraj, K., et al. (2014). Ethenoguanines undergo glycosylation by nucleoside 2′-deoxyribosyltransferases at non-natural sites. PLoS ONE 9:e115082. doi: 10.1371/journal.pone.0115082spa
dc.relation.referencesZhao, G., Wu, G., Zhang, Y., Liu, G., Han, T., Deng, Z., et al. (2014). Structure of the N-glycosidase MilB in complex with hydroxymethyl CMP reveals its Arg23 specifically recognizes the substrate and controls its entry. Nucleic Acids Res. 42, 8115–8124. doi: 10.1093/nar/gku486spa
dc.relation.referencesZhou, X., Yan, W., Zhang, C., Yang, Z., Neubauer, P., Mikhailopulo, I. A., et al. (2019). Biocatalytic synthesis of seleno-, thio-and chloro-nucleobase modified nucleosides by thermostable nucleoside phosphorylases. Catal. Commun. 121, 32–37. doi: 10.1016/j.catcom.2018.12.004spa
dc.type.coarhttp://purl.org/coar/resource_type/c_6501spa
dc.type.contentTextspa
dc.type.driverinfo:eu-repo/semantics/articlespa
dc.type.redcolhttp://purl.org/redcol/resource_type/ARTspa
dc.type.versioninfo:eu-repo/semantics/acceptedVersionspa
dc.type.coarversionhttp://purl.org/coar/version/c_ab4af688f83e57aaspa
dc.rights.coarhttp://purl.org/coar/access_right/c_abf2spa


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