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N-Ribosyltransferase From Archaeoglobus veneficus: A Novel Halotolerant and Thermostable Biocatalyst for the Synthesis of Purine Ribonucleoside Analogs
dc.contributor.author | Acosta, Javier | spa |
dc.contributor.author | Del Arco, Jon | spa |
dc.contributor.author | Pisabarro, Victor | spa |
dc.contributor.author | Gago, Federico | spa |
dc.contributor.author | Fernández-Lucas, Jesús | spa |
dc.date.accessioned | 2020-07-07T19:15:03Z | |
dc.date.available | 2020-07-07T19:15:03Z | |
dc.date.issued | 2020-06-20 | |
dc.identifier.issn | 2296-4185 | spa |
dc.identifier.uri | https://hdl.handle.net/11323/6474 | spa |
dc.description.abstract | Nucleoside-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.iso | eng | |
dc.publisher | Frontiers in Bioengineering and Biotechnology | spa |
dc.rights | CC0 1.0 Universal | spa |
dc.rights.uri | http://creativecommons.org/publicdomain/zero/1.0/ | spa |
dc.subject | Nucleosides | spa |
dc.subject | Extremophiles | spa |
dc.subject | Nucleoside 2′-deoxyribosyltransferase | spa |
dc.subject | Transglycosylation | spa |
dc.subject | Homology modeling | spa |
dc.title | N-Ribosyltransferase From Archaeoglobus veneficus: A Novel Halotolerant and Thermostable Biocatalyst for the Synthesis of Purine Ribonucleoside Analogs | spa |
dc.type | Artículo de revista | spa |
dc.rights.accessrights | info:eu-repo/semantics/openAccess | spa |
dc.identifier.doi | https://doi.org/10.3389/fbioe.2020.00593 | spa |
dc.identifier.instname | Corporación Universidad de la Costa | spa |
dc.identifier.reponame | REDICUC - Repositorio CUC | spa |
dc.identifier.repourl | https://repositorio.cuc.edu.co/ | spa |
dc.relation.references | Thomson, J., and Lamont, I. (2019). Nucleoside analogues as antibacterial agents. Front. Microbiol. 10:952. doi: 10.3389/fmicb.2019.00952 | spa |
dc.relation.references | Trelles, 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.references | Vichier-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/c7ob01850a | spa |
dc.relation.references | Ye, 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.0115082 | spa |
dc.relation.references | Zhao, 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/gku486 | spa |
dc.relation.references | Zhou, 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.2018.12.004 | spa |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | spa |
dc.type.content | Text | spa |
dc.type.driver | info:eu-repo/semantics/article | spa |
dc.type.redcol | http://purl.org/redcol/resource_type/ART | spa |
dc.type.version | info:eu-repo/semantics/acceptedVersion | spa |
dc.type.coarversion | http://purl.org/coar/version/c_ab4af688f83e57aa | spa |
dc.rights.coar | http://purl.org/coar/access_right/c_abf2 | spa |
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