N-Ribosyltransferase From Archaeoglobus veneficus: A Novel Halotolerant and Thermostable Biocatalyst for the Synthesis of Purine Ribonucleoside Analogs
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...
- Autores:
-
Acosta, Javier
Del Arco, Jon
Pisabarro, Victor
Gago, Federico
Fernández-Lucas, Jesús
- Tipo de recurso:
- Article of journal
- Fecha de publicación:
- 2020
- Institución:
- Corporación Universidad de la Costa
- Repositorio:
- REDICUC - Repositorio CUC
- Idioma:
- eng
- OAI Identifier:
- oai:repositorio.cuc.edu.co:11323/6474
- Acceso en línea:
- https://hdl.handle.net/11323/6474
https://doi.org/10.3389/fbioe.2020.00593
https://repositorio.cuc.edu.co/
- Palabra clave:
- Nucleosides
Extremophiles
Nucleoside 2′-deoxyribosyltransferase
Transglycosylation
Homology modeling
- Rights
- openAccess
- License
- CC0 1.0 Universal
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| dc.title.spa.fl_str_mv |
N-Ribosyltransferase From Archaeoglobus veneficus: A Novel Halotolerant and Thermostable Biocatalyst for the Synthesis of Purine Ribonucleoside Analogs |
| title |
N-Ribosyltransferase From Archaeoglobus veneficus: A Novel Halotolerant and Thermostable Biocatalyst for the Synthesis of Purine Ribonucleoside Analogs |
| spellingShingle |
N-Ribosyltransferase From Archaeoglobus veneficus: A Novel Halotolerant and Thermostable Biocatalyst for the Synthesis of Purine Ribonucleoside Analogs Nucleosides Extremophiles Nucleoside 2′-deoxyribosyltransferase Transglycosylation Homology modeling |
| title_short |
N-Ribosyltransferase From Archaeoglobus veneficus: A Novel Halotolerant and Thermostable Biocatalyst for the Synthesis of Purine Ribonucleoside Analogs |
| title_full |
N-Ribosyltransferase From Archaeoglobus veneficus: A Novel Halotolerant and Thermostable Biocatalyst for the Synthesis of Purine Ribonucleoside Analogs |
| title_fullStr |
N-Ribosyltransferase From Archaeoglobus veneficus: A Novel Halotolerant and Thermostable Biocatalyst for the Synthesis of Purine Ribonucleoside Analogs |
| title_full_unstemmed |
N-Ribosyltransferase From Archaeoglobus veneficus: A Novel Halotolerant and Thermostable Biocatalyst for the Synthesis of Purine Ribonucleoside Analogs |
| title_sort |
N-Ribosyltransferase From Archaeoglobus veneficus: A Novel Halotolerant and Thermostable Biocatalyst for the Synthesis of Purine Ribonucleoside Analogs |
| dc.creator.fl_str_mv |
Acosta, Javier Del Arco, Jon Pisabarro, Victor Gago, Federico Fernández-Lucas, Jesús |
| dc.contributor.author.spa.fl_str_mv |
Acosta, Javier Del Arco, Jon Pisabarro, Victor Gago, Federico Fernández-Lucas, Jesús |
| dc.subject.spa.fl_str_mv |
Nucleosides Extremophiles Nucleoside 2′-deoxyribosyltransferase Transglycosylation Homology modeling |
| topic |
Nucleosides Extremophiles Nucleoside 2′-deoxyribosyltransferase Transglycosylation Homology modeling |
| description |
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. |
| publishDate |
2020 |
| dc.date.accessioned.none.fl_str_mv |
2020-07-07T19:15:03Z |
| dc.date.available.none.fl_str_mv |
2020-07-07T19:15:03Z |
| dc.date.issued.none.fl_str_mv |
2020-06-20 |
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Artículo de revista |
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http://purl.org/coar/resource_type/c_2df8fbb1 |
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http://purl.org/coar/resource_type/c_6501 |
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Text |
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info:eu-repo/semantics/article |
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http://purl.org/redcol/resource_type/ART |
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acceptedVersion |
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2296-4185 |
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https://hdl.handle.net/11323/6474 |
| dc.identifier.doi.spa.fl_str_mv |
https://doi.org/10.3389/fbioe.2020.00593 |
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Corporación Universidad de la Costa |
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REDICUC - Repositorio CUC |
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https://repositorio.cuc.edu.co/ |
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2296-4185 Corporación Universidad de la Costa REDICUC - Repositorio CUC |
| url |
https://hdl.handle.net/11323/6474 https://doi.org/10.3389/fbioe.2020.00593 https://repositorio.cuc.edu.co/ |
| dc.language.iso.none.fl_str_mv |
eng |
| language |
eng |
| dc.relation.references.spa.fl_str_mv |
Thomson, J., and Lamont, I. (2019). Nucleoside analogues as antibacterial agents. Front. Microbiol. 10:952. doi: 10.3389/fmicb.2019.00952 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. 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 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 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 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 |
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CC0 1.0 Universal |
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http://creativecommons.org/publicdomain/zero/1.0/ |
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Frontiers in Bioengineering and Biotechnology |
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Acosta, JavierDel Arco, JonPisabarro, VictorGago, FedericoFernández-Lucas, Jesús2020-07-07T19:15:03Z2020-07-07T19:15:03Z2020-06-202296-4185https://hdl.handle.net/11323/6474https://doi.org/10.3389/fbioe.2020.00593Corporación Universidad de la CostaREDICUC - Repositorio CUChttps://repositorio.cuc.edu.co/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.Acosta, JavierDel Arco, JonPisabarro, VictorGago, FedericoFernández-Lucas, JesúsengFrontiers in Bioengineering and BiotechnologyCC0 1.0 Universalhttp://creativecommons.org/publicdomain/zero/1.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2NucleosidesExtremophilesNucleoside 2′-deoxyribosyltransferaseTransglycosylationHomology modelingN-Ribosyltransferase From Archaeoglobus veneficus: A Novel Halotolerant and Thermostable Biocatalyst for the Synthesis of Purine Ribonucleoside AnalogsArtículo de revistahttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1Textinfo:eu-repo/semantics/articlehttp://purl.org/redcol/resource_type/ARTinfo:eu-repo/semantics/acceptedVersionThomson, J., and Lamont, I. (2019). Nucleoside analogues as antibacterial agents. Front. Microbiol. 10:952. doi: 10.3389/fmicb.2019.00952Trelles, 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.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/c7ob01850aYe, 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.0115082Zhao, 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/gku486Zhou, 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. 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