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Structural and functional characterization of thermostable biocatalysts for the synthesis of 6-aminopurine nucleoside-5′-monophospate analogues
| dc.contributor.author | Del Arco, Jon | spa |
| dc.contributor.author | Pérez, Elena | spa |
| dc.contributor.author | Naitow, Hisashi | spa |
| dc.contributor.author | Matsuura, Yoshinori | spa |
| dc.contributor.author | Kunishima, Naoki | spa |
| dc.contributor.author | Fernández-Lucas, Jesús | spa |
| dc.date.accessioned | 2019-05-15T12:59:05Z | |
| dc.date.available | 2019-05-15T12:59:05Z | |
| dc.date.issued | 2019-01-03 | |
| dc.identifier.uri | http://hdl.handle.net/11323/3330 | spa |
| dc.description.abstract | The present work describes the functional and structural characterization of adenine phosphoribosyltransferase 2 from thermus thermophilus hb8 (ttaprt2). The combination of structural and substrate specificity data provided valuable information for immobilization studies. Dimeric ttaprt2 was immobilized onto glutaraldehydeactivated magresyn®amine magnetic iron oxide porous microparticles by two different strategies: a) an enzyme immobilization at ph 8.5 to encourage the immobilization process by n-termini (mttaprt2a, mttaprt2b, mttaprt2c) or b) an enzyme immobilization at ph 10.0 to encourage the immobilization process through surface exposed lysine residues (mttaprt2d, mttaprt2e, mttaprt2f). According to catalyst load experiments, mttaprt2b (activity: 480 iu g−1 biocatalyst, activity recovery: 52%) and mttaprt2f (activity: 507 iu g−1 biocatalyst, activity recovery: 44%) were chosen as optimal derivatives. The biochemical characterization studies demonstrated that immobilization process improved the thermostability of ttaprt2. Moreover, the potential reusability of mttaprt2b and mttaprt2f was also tested. Finally, mttaprt2f was employed in the synthesis of nucleoside-5′-monophosphate analogues. | spa |
| dc.description.abstract | El presente trabajo describe la caracterización funcional y estructural de la adenina fosforribosiltransferasa 2 de thermus thermophilus hb8 (ttaprt2). La combinación de datos de especificidad estructural y de sustrato proporcionó información valiosa para los estudios de inmovilización. El ttaprt2 dimérico se inmovilizó en micropartículas porosas de óxido de hierro magnético magresyn®amine activado con glutaraldehido mediante dos estrategias diferentes: a) una inmovilización de enzima a ph 8.5 para alentar el proceso de inmovilización por n-termini (mttaprt2a, mttaprt2c) o bttaprt2c) o b) ph 10.0 para fomentar el proceso de inmovilización a través de residuos de lisina expuestos en la superficie (mttaprt2d, mttaprt2e, mttaprt2f). De acuerdo con los experimentos de carga de catalizador, mttaprt2b (actividad: 480 iu g − 1 biocatalizador, recuperación de actividad: 52%) y mttaprt2f (actividad: 507 iu g − 1 biocatalizador, recuperación de actividad: 44%) fueron elegidos como derivados óptimos. Los estudios de caracterización bioquímica demostraron que el proceso de inmovilización mejoró la termoestabilidad de ttaprt2. Además, también se probó la reutilización potencial de mttaprt2b y mttaprt2f. Finalmente, mttaprt2f se empleó en la síntesis de análogos de nucleósido-5'-monofosfato. | spa |
| dc.language.iso | eng | |
| dc.publisher | Universidad de la Costa | spa |
| dc.rights | Attribution-NonCommercial-ShareAlike 4.0 International | spa |
| dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | spa |
| dc.subject | Thermophiles | spa |
| dc.subject | Biocatalysis | spa |
| dc.subject | Enzyme immobilization | spa |
| dc.subject | Protein crystallography | spa |
| dc.subject | Termofilos | spa |
| dc.subject | Biocatálisis | spa |
| dc.subject | Inmovilización de enzimas | spa |
| dc.subject | Cristalografia de proteinas | spa |
| dc.title | Structural and functional characterization of thermostable biocatalysts for the synthesis of 6-aminopurine nucleoside-5′-monophospate analogues | spa |
| dc.type | Artículo de revista | spa |
| dc.rights.accessrights | info:eu-repo/semantics/openAccess | 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 |
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| dc.title.translated | Caracterización estructural y funcional de biocatalizadores termoestables para la síntesis de análogos del nucleósido 5'-monofosfato de 6-aminopurina. | 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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