Characterization Of An Atypical, Thermostable, Organic Solvent- And Acid-Tolerant 2′-Deoxyribosyltransferase From Chroococcidiopsis Thermalis
In our search for thermophilic and acid-tolerant nucleoside 2′-deoxyribosyltransferases (NDTs), we found a good candidate in an enzyme encoded by Chroococcidiopsis thermalis PCC 7203 (CtNDT). Biophysical and biochemical characterization revealed CtNDT as a homotetramer endowed with good activity and...
- Autores:
-
Del Arco, Jon
Sánchez Murcia, Pedro Alejandro
Mancheño José Miguel, José Miguel
Gago, Federico
Fernandez Lucas, Jesus
- Tipo de recurso:
- Article of journal
- Fecha de publicación:
- 2018
- Institución:
- Corporación Universidad de la Costa
- Repositorio:
- REDICUC - Repositorio CUC
- Idioma:
- eng
- OAI Identifier:
- oai:repositorio.cuc.edu.co:11323/1093
- Acceso en línea:
- https://hdl.handle.net/11323/1093
https://repositorio.cuc.edu.co/
- Palabra clave:
- Enzymatic Synthesis
Extremophiles
Homology Modeling
Nucleoside 2′-Deoxyribosyltransferase
Nucleoside Analogues
- Rights
- openAccess
- License
- Atribución – No comercial – Compartir igual
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|
dc.title.eng.fl_str_mv |
Characterization Of An Atypical, Thermostable, Organic Solvent- And Acid-Tolerant 2′-Deoxyribosyltransferase From Chroococcidiopsis Thermalis |
title |
Characterization Of An Atypical, Thermostable, Organic Solvent- And Acid-Tolerant 2′-Deoxyribosyltransferase From Chroococcidiopsis Thermalis |
spellingShingle |
Characterization Of An Atypical, Thermostable, Organic Solvent- And Acid-Tolerant 2′-Deoxyribosyltransferase From Chroococcidiopsis Thermalis Enzymatic Synthesis Extremophiles Homology Modeling Nucleoside 2′-Deoxyribosyltransferase Nucleoside Analogues |
title_short |
Characterization Of An Atypical, Thermostable, Organic Solvent- And Acid-Tolerant 2′-Deoxyribosyltransferase From Chroococcidiopsis Thermalis |
title_full |
Characterization Of An Atypical, Thermostable, Organic Solvent- And Acid-Tolerant 2′-Deoxyribosyltransferase From Chroococcidiopsis Thermalis |
title_fullStr |
Characterization Of An Atypical, Thermostable, Organic Solvent- And Acid-Tolerant 2′-Deoxyribosyltransferase From Chroococcidiopsis Thermalis |
title_full_unstemmed |
Characterization Of An Atypical, Thermostable, Organic Solvent- And Acid-Tolerant 2′-Deoxyribosyltransferase From Chroococcidiopsis Thermalis |
title_sort |
Characterization Of An Atypical, Thermostable, Organic Solvent- And Acid-Tolerant 2′-Deoxyribosyltransferase From Chroococcidiopsis Thermalis |
dc.creator.fl_str_mv |
Del Arco, Jon Sánchez Murcia, Pedro Alejandro Mancheño José Miguel, José Miguel Gago, Federico Fernandez Lucas, Jesus |
dc.contributor.author.spa.fl_str_mv |
Del Arco, Jon Sánchez Murcia, Pedro Alejandro Mancheño José Miguel, José Miguel Gago, Federico Fernandez Lucas, Jesus |
dc.subject.eng.fl_str_mv |
Enzymatic Synthesis Extremophiles Homology Modeling Nucleoside 2′-Deoxyribosyltransferase Nucleoside Analogues |
topic |
Enzymatic Synthesis Extremophiles Homology Modeling Nucleoside 2′-Deoxyribosyltransferase Nucleoside Analogues |
description |
In our search for thermophilic and acid-tolerant nucleoside 2′-deoxyribosyltransferases (NDTs), we found a good candidate in an enzyme encoded by Chroococcidiopsis thermalis PCC 7203 (CtNDT). Biophysical and biochemical characterization revealed CtNDT as a homotetramer endowed with good activity and stability at both high temperatures (50–100 °C) and a wide range of pH values (from 3 to 7). CtNDT recognizes purine bases and their corresponding 2′-deoxynucleosides but is also proficient using cytosine and 2′-deoxycytidine as substrates. These unusual features preclude the strict classification of CtNDT as either a type I or a type II NDT and further suggest that this simple subdivision may need to be updated in the future. Our findings also hint at a possible link between oligomeric state and NDT’s substrate specificity. Interestingly from a practical perspective, CtNDT displays high activity (80–100%) in the presence of several water-miscible co-solvents in a proportion of up to 20% and was successfully employed in the enzymatic production of several therapeutic nucleosides such as didanosine, vidarabine, and cytarabine. |
publishDate |
2018 |
dc.date.accessioned.none.fl_str_mv |
2018-11-16T01:03:25Z |
dc.date.available.none.fl_str_mv |
2018-11-16T01:03:25Z |
dc.date.issued.none.fl_str_mv |
2018-05-23 |
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 |
0175-7598 |
dc.identifier.uri.spa.fl_str_mv |
https://hdl.handle.net/11323/1093 |
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 |
0175-7598 Corporación Universidad de la Costa REDICUC - Repositorio CUC |
url |
https://hdl.handle.net/11323/1093 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 |
Applied Microbiology And Biotechnology |
institution |
Corporación Universidad de la Costa |
bitstream.url.fl_str_mv |
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1828166890285957120 |
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Del Arco, JonSánchez Murcia, Pedro AlejandroMancheño José Miguel, José MiguelGago, FedericoFernandez Lucas, Jesus2018-11-16T01:03:25Z2018-11-16T01:03:25Z2018-05-230175-7598https://hdl.handle.net/11323/1093Corporación Universidad de la CostaREDICUC - Repositorio CUChttps://repositorio.cuc.edu.co/In our search for thermophilic and acid-tolerant nucleoside 2′-deoxyribosyltransferases (NDTs), we found a good candidate in an enzyme encoded by Chroococcidiopsis thermalis PCC 7203 (CtNDT). Biophysical and biochemical characterization revealed CtNDT as a homotetramer endowed with good activity and stability at both high temperatures (50–100 °C) and a wide range of pH values (from 3 to 7). CtNDT recognizes purine bases and their corresponding 2′-deoxynucleosides but is also proficient using cytosine and 2′-deoxycytidine as substrates. These unusual features preclude the strict classification of CtNDT as either a type I or a type II NDT and further suggest that this simple subdivision may need to be updated in the future. Our findings also hint at a possible link between oligomeric state and NDT’s substrate specificity. Interestingly from a practical perspective, CtNDT displays high activity (80–100%) in the presence of several water-miscible co-solvents in a proportion of up to 20% and was successfully employed in the enzymatic production of several therapeutic nucleosides such as didanosine, vidarabine, and cytarabine.Del Arco, Jon-c5ed68af-857c-4b28-99a7-33a4254ed926-600Sánchez Murcia, Pedro Alejandro-36f5facd-580d-4ecb-9ff8-59e541b83d2c-600Mancheño José Miguel, José Miguel-efd44cff-f0f8-4460-8c0c-788bddd07eb8-600Gago, Federico-01869b67-1b3d-442b-b9aa-7ba5beb0de2c-600Fernandez Lucas, Jesus-3f36c351-7522-42ea-8605-cd7e804a6387-600engApplied Microbiology And BiotechnologyAtribución – No comercial – Compartir igualinfo:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Enzymatic SynthesisExtremophilesHomology ModelingNucleoside 2′-DeoxyribosyltransferaseNucleoside AnaloguesCharacterization Of An Atypical, Thermostable, Organic Solvent- And Acid-Tolerant 2′-Deoxyribosyltransferase From Chroococcidiopsis ThermalisArtículo 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/acceptedVersionPublicationORIGINALCharacterization of an atypical.pdfCharacterization of an atypical.pdfapplication/pdf3230938https://repositorio.cuc.edu.co/bitstreams/ddd1c86f-5a2d-4630-add9-29f5521bfaf4/download352206989cfe11ba434d921d4c0f7592MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://repositorio.cuc.edu.co/bitstreams/d567e30b-7c8d-482b-b673-312ea2d8c699/download8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAILCharacterization of an atypical.pdf.jpgCharacterization of an atypical.pdf.jpgimage/jpeg56829https://repositorio.cuc.edu.co/bitstreams/42546afd-396c-4933-b91a-3809fb80d9d3/downloadfca413bff38e7ee65501cc20f99904bcMD54TEXTCharacterization of an atypical.pdf.txtCharacterization of an atypical.pdf.txttext/plain50514https://repositorio.cuc.edu.co/bitstreams/61c6195d-2105-49d4-9c6c-578a6f2184e1/download2134c28b768f11bae780e9a9cb138483MD5511323/1093oai:repositorio.cuc.edu.co:11323/10932024-09-17 14:22:46.646open.accesshttps://repositorio.cuc.edu.coRepositorio de la Universidad de la Costa CUCrepdigital@cuc.edu.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 |