Taylor-made production of pyrimidine nucleoside-5′-monophosphate analogues by highly stabilized mutant uracil phosphoribosyltransferase from Toxoplasma gondii
Nowadays, enzymatic synthesis of nucleotides is an efficient and sustainable alternative to chemical methodologies. In this regard, after the biochemical characterization of wild-type and mutant uracil phosphoribosyltransferases from Toxoplasma gondii (TgUPRT, TgUPRT2, and TgUPRT3), TgUPRT2 was sele...
- Autores:
-
Acosta, Javier
Nguyen, Kim
C. Spitale, Robert
Fernández-Lucas, Jesús
- Tipo de recurso:
- Article of journal
- Fecha de publicación:
- 2021
- Institución:
- Corporación Universidad de la Costa
- Repositorio:
- REDICUC - Repositorio CUC
- Idioma:
- eng
- OAI Identifier:
- oai:repositorio.cuc.edu.co:11323/8625
- Acceso en línea:
- https://hdl.handle.net/11323/8625
https://doi.org/10.1016/j.biortech.2021.125649
https://repositorio.cuc.edu.co/
- Palabra clave:
- Nucleoside-5′-monophosphates
Phosphoribosyltransferases
Structure-guided immobilization
- Rights
- embargoedAccess
- License
- CC0 1.0 Universal
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| dc.title.spa.fl_str_mv |
Taylor-made production of pyrimidine nucleoside-5′-monophosphate analogues by highly stabilized mutant uracil phosphoribosyltransferase from Toxoplasma gondii |
| title |
Taylor-made production of pyrimidine nucleoside-5′-monophosphate analogues by highly stabilized mutant uracil phosphoribosyltransferase from Toxoplasma gondii |
| spellingShingle |
Taylor-made production of pyrimidine nucleoside-5′-monophosphate analogues by highly stabilized mutant uracil phosphoribosyltransferase from Toxoplasma gondii Nucleoside-5′-monophosphates Phosphoribosyltransferases Structure-guided immobilization |
| title_short |
Taylor-made production of pyrimidine nucleoside-5′-monophosphate analogues by highly stabilized mutant uracil phosphoribosyltransferase from Toxoplasma gondii |
| title_full |
Taylor-made production of pyrimidine nucleoside-5′-monophosphate analogues by highly stabilized mutant uracil phosphoribosyltransferase from Toxoplasma gondii |
| title_fullStr |
Taylor-made production of pyrimidine nucleoside-5′-monophosphate analogues by highly stabilized mutant uracil phosphoribosyltransferase from Toxoplasma gondii |
| title_full_unstemmed |
Taylor-made production of pyrimidine nucleoside-5′-monophosphate analogues by highly stabilized mutant uracil phosphoribosyltransferase from Toxoplasma gondii |
| title_sort |
Taylor-made production of pyrimidine nucleoside-5′-monophosphate analogues by highly stabilized mutant uracil phosphoribosyltransferase from Toxoplasma gondii |
| dc.creator.fl_str_mv |
Acosta, Javier Nguyen, Kim C. Spitale, Robert Fernández-Lucas, Jesús |
| dc.contributor.author.spa.fl_str_mv |
Acosta, Javier Nguyen, Kim C. Spitale, Robert Fernández-Lucas, Jesús |
| dc.subject.spa.fl_str_mv |
Nucleoside-5′-monophosphates Phosphoribosyltransferases Structure-guided immobilization |
| topic |
Nucleoside-5′-monophosphates Phosphoribosyltransferases Structure-guided immobilization |
| description |
Nowadays, enzymatic synthesis of nucleotides is an efficient and sustainable alternative to chemical methodologies. In this regard, after the biochemical characterization of wild-type and mutant uracil phosphoribosyltransferases from Toxoplasma gondii (TgUPRT, TgUPRT2, and TgUPRT3), TgUPRT2 was selected as the optimal candidate (69.5 IU mg−1, UMP synthesis) for structure-guided immobilization onto Ni2+ chelate (MNiUPRT2) and onto glutaraldehyde-activated microparticles (MGlUPRT2). Among resulting derivatives, MNiUPRT23 (6127 IU g−1biocat; 92% retained activity; 3–5 fold enhanced stability at 50–60 °C) and MGlUPRT2N (3711 IU g−1biocat; 27% retained activity; 8–20 fold enhanced stability at 50–60 °C) displayed the best operability. Moreover, the enzymatic synthesis of different pyrimidine NMPs was performed. Finally, the reusability of both derivatives in 5-FUMP synthesis (MNiUPRT23, 80% retained activity after 7 cycles, 5 min; MGlUPRT2N, 70% retained activity after 10 cycles, 20 min) was carried out at short times. © 2021 Elsevier Ltd |
| publishDate |
2021 |
| dc.date.accessioned.none.fl_str_mv |
2021-09-03T17:01:58Z |
| dc.date.available.none.fl_str_mv |
2021-09-03T17:01:58Z |
| dc.date.issued.none.fl_str_mv |
2021 |
| dc.date.embargoEnd.none.fl_str_mv |
2023-07-21 |
| dc.type.spa.fl_str_mv |
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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http://purl.org/redcol/resource_type/ART |
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info:eu-repo/semantics/acceptedVersion |
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09608524 |
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https://hdl.handle.net/11323/8625 |
| dc.identifier.doi.spa.fl_str_mv |
https://doi.org/10.1016/j.biortech.2021.125649 |
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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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09608524 Corporación Universidad de la Costa REDICUC - Repositorio CUC |
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https://hdl.handle.net/11323/8625 https://doi.org/10.1016/j.biortech.2021.125649 https://repositorio.cuc.edu.co/ |
| dc.language.iso.none.fl_str_mv |
eng |
| language |
eng |
| dc.relation.references.spa.fl_str_mv |
Acosta, J., Del Arco, J., Martinez-Pascual, S., Clemente-Suarez, ´ V.J., Fernandez-Lucas, ´ J., 2018. One-pot multi-enzymatic production of purine derivatives with application in pharmaceutical and food industry. Catalysts 8, 9. https://doi.org/10.3390/ catal8010009. Acosta, J., Del Arco, J., Pisabarro, V., Gago, F., Fernandez-Lucas, ´ J., 2020a. Nribosyltransferase from Archaeoglobus veneficus: a novel halotolerant and thermostable biocatalyst for the synthesis of purine ribonucleoside analogs. Front. Bioeng. Biotechnol. 8, 593. https://doi.org/10.3389/fbioe.2020.00593. Acosta, J., Del Arco, J., Del Pozo, M.L., Herrera-Tapias, B., Clemente-Suarez, ´ V.J., Berenguer, J., Hidalgo, A., Fernandez-Lucas, ´ J., 2020b. Hypoxanthine-guanine phosphoribosyltransferase/adenylate kinase from Zobellia galactanivorans: a bifunctional catalyst for the synthesis of nucleoside-5′ -mono-, di-and triphosphates. Front. Bioeng. Biotechnol. 8, 677. https://doi.org/10.3389/fbioe.2020.00677. Acosta, J., Del Arco, J., Del Pozo, M.L., Herrera-Tapias, B., Clemente-Suarez, ´ V.J., Berenguer, J., Hidalgo, A., Fernandez-Lucas, ´ J., 2020b. Hypoxanthine-guanine phosphoribosyltransferase/adenylate kinase from Zobellia galactanivorans: a bifunctional catalyst for the synthesis of nucleoside-5′ -mono-, di-and triphosphates. Front. Bioeng. Biotechnol. 8, 677. https://doi.org/10.3389/fbioe.2020.00677. Acosta, J., Del Arco, J., Del Pozo, M.L., Herrera-Tapias, B., Clemente-Suarez, ´ V.J., Berenguer, J., Hidalgo, A., Fernandez-Lucas, ´ J., 2020b. Hypoxanthine-guanine phosphoribosyltransferase/adenylate kinase from Zobellia galactanivorans: a bifunctional catalyst for the synthesis of nucleoside-5′ -mono-, di-and triphosphates. Front. Bioeng. Biotechnol. 8, 677. https://doi.org/10.3389/fbioe.2020.00677. Al-Qodah, Z., Al-Shannag, M., Al-Bosoul, M., Penchev, I., Al-Ahmadi, H., Al-Qodah, K., 2018. On the performance of immobilized cell bioreactors utilizing a magnetic field. Rev. Chem. 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Enzymatic production of non-natural nucleoside-5’- monophosphates by a novel thermostable uracil phosphoribosyltransferase. ChemCatChem 10, 439–448. https://doi.org/10.1002/cctc.201701223. Del Arco, J., Martínez-Pascual, S., Clemente-Su´ arez, V.J., Corral, O.J., Jordaan, J., Hormigo, D., Perona, A., Fern´ andez-Lucas, J., 2018c. One-pot, one-step production of dietary nucleotides by magnetic biocatalysts. Catalysts 8, 184. https://doi.org/ 10.3390/catal8050184. Del Arco, J., Jordaan, J., Moral-Dard´e, V., Fernandez-Lucas, ´ J., 2019a. Sustainable production of nucleoside analogues by a high-efficient purine 2‘- deoxyribosyltransferase immobilized onto Ni2+ chelate magnetic microparticles. Bioresour. Technol. 289, 121772. https://doi.org/10.1016/j.biortech.2019.121772. Del Arco, J., P´erez, E., Naitow, H., Matsuura, Y., Kunishima, N., Fernandez-Lucas, ´ J., 2019b. Structural and functional characterization of thermostable biocatalysts for the synthesis of 6-aminopurine nucleoside-5′ -monophospate analogues. Bioresour. Technol. 276, 244–252. https://doi.org/10.1016/j.biortech.2018.12.120. Del Arco, J., Galindo, J., Clemente-Su´ arez, V.J., Corrales, A., Fern´ andez-Lucas, J., 2020. Sustainable synthesis of uridine-5′ -monophosphate analoguesues by immobilized uracil phosphoribosyltransferase from thermus thermophilus. Biochim. Biophys. Acta Proteins Proteom. 1868, 140251 https://doi.org/10.1016/j.bbapap.2019.07.004. Del Arco, J., Alcantara, ´ A.R., Fernandez-Lafuente, ´ R., Fernandez-Lucas, ´ J., 2021a. Magnetic micro-macro biocatalysts applied to industrial bioprocesses. Bioresour. Technol. 322, 124547. https://doi.org/10.1016/j.biortech.2020.124547. Del Arco, J., Acosta, J., Fern´ andez-Lucas, J., 2021b. New trends in the biocatalytic production of nucleosidic active pharmaceutical ingredients using 2’- deoxyribosyltransferases. Biotechnol. Adv. 107701. https://doi.org/10.1016/j. biotechadv.2021.107701. DeLano, W.L., 2002. The PyMOL Molecular Graphics System. Delano Scientific, San Carlos. Fateev, I.V., Sinitsina, E.V., Bikanasova, A.U., Kostromina, M.A., Tuzova, E.S., Esipova, L. V., Muravyova, T.I., Kayushin, A.L., Konstantinova, I.D., Esipov, R.S., 2018. Thermophilic phosphoribosyltransferases thermus thermophilus HB27 in nucleotide synthesis. Beilstein J. Org. Chem. 14, 3098–3105. https://doi.org/10.3762/ bjoc.14.289. Fernandez-Lafuente, R., 2009. Stabilization of multimeric enzymes: strategies to prevent subunit dissociation. Enzyme Microb. Technol. 45 (6-7), 405–418. https://doi.org/ 10.1016/j.enzmictec.2009.08.009. Fern´ andez-Lucas, J., Harris, R., Mata-Ca Fern´ andez-Lucas, J., Harris, R., Mata-Casar, I., Heras, A., de la Mata, I., Arroyo, M., 2013. Magnetic chitosan beads for covalent immobilization of nucleoside 2’- deoxyribosyltransferase: application in nucleoside analogues synthesis. J. Ind. Microbiol. 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Interaction studies of E. coli uracil phosphoribosyltransferase with 5-fluorouracil for potent anti cancer activity. Med. Chem. Res. 21 (7), 1149–1155. https://doi.org/10.1007/s00044-011-9627-z. Yoshikawa, M., Kato, T., Takenishi, T., 1969. Studies of phosphorylation. III. selective phosphorylation of unprotected nucleosides. Bull. Chem. Soc. Jpn. 42 (12), 3505–3508. https://doi.org/10.1246/bcsj.42.3505. Zou, H., Cai, G., Cai, W., Li, H., Gu, Y., Park, Y., Meng, F., 2008. Extraction and DNA digestion of 5′ -phosphodiesterase from malt root. Tsinghua Sci. Technol. 13 (4), 480–484. https://doi.org/10.1016/S1007-0214(08)70077-4. Zou, Z., Ding, Q., Ou, L., Yan, B., 2013. Efficient production of deoxynucleoside-5′ - monophosphates using deoxynucleoside kinase coupled with a GTP-regeneration system. Appl. Microbiol. Biotechnol. 97 (21), 9389–9395. https://doi.org/10.1007/ s00253-013-5173-6. |
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Acosta, JavierNguyen, KimC. Spitale, RobertFernández-Lucas, Jesús2021-09-03T17:01:58Z2021-09-03T17:01:58Z20212023-07-2109608524https://hdl.handle.net/11323/8625https://doi.org/10.1016/j.biortech.2021.125649Corporación Universidad de la CostaREDICUC - Repositorio CUChttps://repositorio.cuc.edu.co/Nowadays, enzymatic synthesis of nucleotides is an efficient and sustainable alternative to chemical methodologies. In this regard, after the biochemical characterization of wild-type and mutant uracil phosphoribosyltransferases from Toxoplasma gondii (TgUPRT, TgUPRT2, and TgUPRT3), TgUPRT2 was selected as the optimal candidate (69.5 IU mg−1, UMP synthesis) for structure-guided immobilization onto Ni2+ chelate (MNiUPRT2) and onto glutaraldehyde-activated microparticles (MGlUPRT2). Among resulting derivatives, MNiUPRT23 (6127 IU g−1biocat; 92% retained activity; 3–5 fold enhanced stability at 50–60 °C) and MGlUPRT2N (3711 IU g−1biocat; 27% retained activity; 8–20 fold enhanced stability at 50–60 °C) displayed the best operability. Moreover, the enzymatic synthesis of different pyrimidine NMPs was performed. Finally, the reusability of both derivatives in 5-FUMP synthesis (MNiUPRT23, 80% retained activity after 7 cycles, 5 min; MGlUPRT2N, 70% retained activity after 10 cycles, 20 min) was carried out at short times. © 2021 Elsevier LtdAcosta, Javier-will be generated-orcid-0000-0002-7710-5703-600Nguyen, KimC. Spitale, RobertFernández-Lucas, Jesús-will be generated-orcid-0000-0001-7045-8306-600application/pdfengBioresource TechnologyCC0 1.0 Universalhttp://creativecommons.org/publicdomain/zero/1.0/info:eu-repo/semantics/embargoedAccesshttp://purl.org/coar/access_right/c_f1cfBioresource Technologyhttps://www.sciencedirect.com/science/article/pii/S0960852421009901Nucleoside-5′-monophosphatesPhosphoribosyltransferasesStructure-guided immobilizationTaylor-made production of pyrimidine nucleoside-5′-monophosphate analogues by highly stabilized mutant uracil phosphoribosyltransferase from Toxoplasma gondiiArtículo 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/acceptedVersionAcosta, J., Del Arco, J., Martinez-Pascual, S., Clemente-Suarez, ´ V.J., Fernandez-Lucas, ´ J., 2018. 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Biotechnol. 97 (21), 9389–9395. https://doi.org/10.1007/ s00253-013-5173-6.PublicationORIGINALTAYLOR-MADE PRODUCTION OF PYRIMIDINE NUCLEOSIDE-5′-MONOPHOSPHATE ANALOGUES BY HIGHLY STABILIZED MUTANT URACIL PHOSPHORIBOSYLTRANSFERASE FROM TOXOPLASMA GONDII.pdfTAYLOR-MADE PRODUCTION OF PYRIMIDINE NUCLEOSIDE-5′-MONOPHOSPHATE ANALOGUES BY HIGHLY STABILIZED MUTANT URACIL PHOSPHORIBOSYLTRANSFERASE FROM TOXOPLASMA GONDII.pdfapplication/pdf91479https://repositorio.cuc.edu.co/bitstreams/95adbd38-0e36-4ad5-afaf-52d747434895/download06bbc2bd63f9d75af986e43ea420ae4eMD51CC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8701https://repositorio.cuc.edu.co/bitstreams/ab400bae-5814-4188-8509-764ed7b9cbdd/download42fd4ad1e89814f5e4a476b409eb708cMD52LICENSElicense.txtlicense.txttext/plain; charset=utf-83196https://repositorio.cuc.edu.co/bitstreams/8cebe51b-dba6-4c56-9673-bfec30d4457b/downloade30e9215131d99561d40d6b0abbe9badMD53THUMBNAILTAYLOR-MADE PRODUCTION OF PYRIMIDINE 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