Purine and pyrimidine phosphoribosyltransferases: A versatile tool for enzymatic synthesis of nucleoside-5′-monophosphates
ackground: In recent years, enzymatic methods have shown to be an efficient and sustainable alternative for the synthesis of nucleosides and nucleoside-5′-monophosphates (NMPs) to the traditional multistep chemical methods, since chemical glycosylation reactions include several protection-deprotecti...
- Autores:
-
Del Arco, Jon
Fernandez Lucas, Jesus
- Tipo de recurso:
- Article of journal
- Fecha de publicación:
- 2017
- Institución:
- Corporación Universidad de la Costa
- Repositorio:
- REDICUC - Repositorio CUC
- Idioma:
- eng
- OAI Identifier:
- oai:repositorio.cuc.edu.co:11323/2239
- Acceso en línea:
- https://hdl.handle.net/11323/2239
https://repositorio.cuc.edu.co/
- Palabra clave:
- Biocatalysis
Nucleic acid derivatives
Nucleoside-5′-monophosphates (NMPs)
Nucleosides
Phosphoribosyltransferase
- Rights
- openAccess
- License
- Atribución – No comercial – Compartir igual
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|
dc.title.spa.fl_str_mv |
Purine and pyrimidine phosphoribosyltransferases: A versatile tool for enzymatic synthesis of nucleoside-5′-monophosphates |
title |
Purine and pyrimidine phosphoribosyltransferases: A versatile tool for enzymatic synthesis of nucleoside-5′-monophosphates |
spellingShingle |
Purine and pyrimidine phosphoribosyltransferases: A versatile tool for enzymatic synthesis of nucleoside-5′-monophosphates Biocatalysis Nucleic acid derivatives Nucleoside-5′-monophosphates (NMPs) Nucleosides Phosphoribosyltransferase |
title_short |
Purine and pyrimidine phosphoribosyltransferases: A versatile tool for enzymatic synthesis of nucleoside-5′-monophosphates |
title_full |
Purine and pyrimidine phosphoribosyltransferases: A versatile tool for enzymatic synthesis of nucleoside-5′-monophosphates |
title_fullStr |
Purine and pyrimidine phosphoribosyltransferases: A versatile tool for enzymatic synthesis of nucleoside-5′-monophosphates |
title_full_unstemmed |
Purine and pyrimidine phosphoribosyltransferases: A versatile tool for enzymatic synthesis of nucleoside-5′-monophosphates |
title_sort |
Purine and pyrimidine phosphoribosyltransferases: A versatile tool for enzymatic synthesis of nucleoside-5′-monophosphates |
dc.creator.fl_str_mv |
Del Arco, Jon Fernandez Lucas, Jesus |
dc.contributor.author.spa.fl_str_mv |
Del Arco, Jon Fernandez Lucas, Jesus |
dc.subject.spa.fl_str_mv |
Biocatalysis Nucleic acid derivatives Nucleoside-5′-monophosphates (NMPs) Nucleosides Phosphoribosyltransferase |
topic |
Biocatalysis Nucleic acid derivatives Nucleoside-5′-monophosphates (NMPs) Nucleosides Phosphoribosyltransferase |
description |
ackground: In recent years, enzymatic methods have shown to be an efficient and sustainable alternative for the synthesis of nucleosides and nucleoside-5′-monophosphates (NMPs) to the traditional multistep chemical methods, since chemical glycosylation reactions include several protection-deprotection steps and the use of chemical reagents and organic solvents that are expensive and environmentally harmful. Results: In this mini-review, we want to illustrate the application of phosphoribosyltransferases (PRTs) in enzymatic synthesis of NMPs. In this sense, many different examples about the use of PRTs as biocatalysts, as whole cells or enzymes, are described. In addition, it also includes detailed comments about structure and catalytic mechanism of described PRTs, as well as their possible biological role and therapeutic use, substrate specificity and advances in detection of new enzyme specificities towards different substrates. In addition, several examples about the use of PRTs in mono or multi-enzymatic synthesis of NMP analogues are shown. Finally, a brief discussion about advantages and drawbacks of the use of PRTs as industrial biocatalyst of NMPs has been commented. Conclusion: Despite the great potential of PRTs as biocatalysts for industrial synthesis of NMPs, several drawbacks must be overcome before reaching a suitable industrial application. In this sense, multi-enzyme systems provide an appropriate framework for this purpose. Moreover, future advances in different disciplines as protein engineering, bioinformatics and -omics will help to reach this goal. |
publishDate |
2017 |
dc.date.issued.none.fl_str_mv |
2017 |
dc.date.accessioned.none.fl_str_mv |
2019-01-25T14:28:25Z |
dc.date.available.none.fl_str_mv |
2019-01-25T14:28:25Z |
dc.type.spa.fl_str_mv |
Artículo de revista |
dc.type.coar.fl_str_mv |
http://purl.org/coar/resource_type/c_2df8fbb1 |
dc.type.coar.spa.fl_str_mv |
http://purl.org/coar/resource_type/c_6501 |
dc.type.content.spa.fl_str_mv |
Text |
dc.type.driver.spa.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.redcol.spa.fl_str_mv |
http://purl.org/redcol/resource_type/ART |
dc.type.version.spa.fl_str_mv |
info:eu-repo/semantics/acceptedVersion |
format |
http://purl.org/coar/resource_type/c_6501 |
status_str |
acceptedVersion |
dc.identifier.issn.spa.fl_str_mv |
13816128 |
dc.identifier.uri.spa.fl_str_mv |
https://hdl.handle.net/11323/2239 |
dc.identifier.instname.spa.fl_str_mv |
Corporación Universidad de la Costa |
dc.identifier.reponame.spa.fl_str_mv |
REDICUC - Repositorio CUC |
dc.identifier.repourl.spa.fl_str_mv |
https://repositorio.cuc.edu.co/ |
identifier_str_mv |
13816128 Corporación Universidad de la Costa REDICUC - Repositorio CUC |
url |
https://hdl.handle.net/11323/2239 https://repositorio.cuc.edu.co/ |
dc.language.iso.none.fl_str_mv |
eng |
language |
eng |
dc.rights.spa.fl_str_mv |
Atribución – No comercial – Compartir igual |
dc.rights.accessrights.spa.fl_str_mv |
info:eu-repo/semantics/openAccess |
dc.rights.coar.spa.fl_str_mv |
http://purl.org/coar/access_right/c_abf2 |
rights_invalid_str_mv |
Atribución – No comercial – Compartir igual http://purl.org/coar/access_right/c_abf2 |
eu_rights_str_mv |
openAccess |
dc.publisher.spa.fl_str_mv |
Current Pharmaceutical Design |
institution |
Corporación Universidad de la Costa |
bitstream.url.fl_str_mv |
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Del Arco, JonFernandez Lucas, Jesus2019-01-25T14:28:25Z2019-01-25T14:28:25Z201713816128https://hdl.handle.net/11323/2239Corporación Universidad de la CostaREDICUC - Repositorio CUChttps://repositorio.cuc.edu.co/ackground: In recent years, enzymatic methods have shown to be an efficient and sustainable alternative for the synthesis of nucleosides and nucleoside-5′-monophosphates (NMPs) to the traditional multistep chemical methods, since chemical glycosylation reactions include several protection-deprotection steps and the use of chemical reagents and organic solvents that are expensive and environmentally harmful. Results: In this mini-review, we want to illustrate the application of phosphoribosyltransferases (PRTs) in enzymatic synthesis of NMPs. In this sense, many different examples about the use of PRTs as biocatalysts, as whole cells or enzymes, are described. In addition, it also includes detailed comments about structure and catalytic mechanism of described PRTs, as well as their possible biological role and therapeutic use, substrate specificity and advances in detection of new enzyme specificities towards different substrates. In addition, several examples about the use of PRTs in mono or multi-enzymatic synthesis of NMP analogues are shown. Finally, a brief discussion about advantages and drawbacks of the use of PRTs as industrial biocatalyst of NMPs has been commented. Conclusion: Despite the great potential of PRTs as biocatalysts for industrial synthesis of NMPs, several drawbacks must be overcome before reaching a suitable industrial application. In this sense, multi-enzyme systems provide an appropriate framework for this purpose. Moreover, future advances in different disciplines as protein engineering, bioinformatics and -omics will help to reach this goal.Del Arco, Jon-c5ed68af-857c-4b28-99a7-33a4254ed926-600Fernandez Lucas, Jesus-3f36c351-7522-42ea-8605-cd7e804a6387-600engCurrent Pharmaceutical DesignAtribución – No comercial – Compartir igualinfo:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2BiocatalysisNucleic acid derivativesNucleoside-5′-monophosphates (NMPs)NucleosidesPhosphoribosyltransferasePurine and pyrimidine phosphoribosyltransferases: A versatile tool for enzymatic synthesis of nucleoside-5′-monophosphatesArtículo 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/acceptedVersionPublicationORIGINALPurine and pyrimidine phosphoribosyltransferases.pdfPurine and pyrimidine phosphoribosyltransferases.pdfapplication/pdf357839https://repositorio.cuc.edu.co/bitstreams/091aa231-3d2b-4c48-8b8e-0872ff55681b/download761ac16c903aee06990bad23a2530255MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://repositorio.cuc.edu.co/bitstreams/6b5d1a9a-681f-4339-a05a-db8a1fce8a79/download8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAILPurine and pyrimidine phosphoribosyltransferases.pdf.jpgPurine and pyrimidine phosphoribosyltransferases.pdf.jpgimage/jpeg54405https://repositorio.cuc.edu.co/bitstreams/bbda777c-ca99-487a-9b14-1813f70d70ca/downloadbab5c2d708134a10548c1f2b2fa1ae2cMD54TEXTPurine and pyrimidine phosphoribosyltransferases.pdf.txtPurine and pyrimidine phosphoribosyltransferases.pdf.txttext/plain1937https://repositorio.cuc.edu.co/bitstreams/23d3c821-7392-48e1-a112-2ca282391265/downloadd18e00aefcbea9dc4d5e75137f54e38eMD5511323/2239oai:repositorio.cuc.edu.co:11323/22392024-09-17 10:59:25.785open.accesshttps://repositorio.cuc.edu.coRepositorio de la Universidad de la Costa CUCrepdigital@cuc.edu.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 |