<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-06-27T15:24:29Z</responseDate><request verb="GetRecord" identifier="oai:docta.ucm.es:20.500.14352/109960" metadataPrefix="mods">https://docta.ucm.es/rest/oai/request</request><GetRecord><record><header><identifier>oai:docta.ucm.es:20.500.14352/109960</identifier><datestamp>2025-03-18T12:49:21Z</datestamp><setSpec>com_20.500.14352_14</setSpec><setSpec>col_20.500.14352_15</setSpec></header><metadata><mods:mods xmlns:mods="http://www.loc.gov/mods/v3" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-1.xsd">
   <mods:name>
      <mods:namePart>Del Arco, Jon</mods:namePart>
   </mods:name>
   <mods:name>
      <mods:namePart>Sánchez-Murcia, Pedro Alejandro</mods:namePart>
   </mods:name>
   <mods:name>
      <mods:namePart>Mancheño Gómez, José Miguel</mods:namePart>
   </mods:name>
   <mods:name>
      <mods:namePart>Gago, Federico</mods:namePart>
   </mods:name>
   <mods:name>
      <mods:namePart>Fernández Lucas, Jesús</mods:namePart>
   </mods:name>
   <mods:extension>
      <mods:dateAvailable encoding="iso8601">2024-11-04T16:41:35Z</mods:dateAvailable>
   </mods:extension>
   <mods:extension>
      <mods:dateAccessioned encoding="iso8601">2024-11-04T16:41:35Z</mods:dateAccessioned>
   </mods:extension>
   <mods:originInfo>
      <mods:dateIssued encoding="iso8601">2018</mods:dateIssued>
   </mods:originInfo>
   <mods:identifier type="citation">Del Arco, J., Sánchez-Murcia, P. A., Mancheño, J. M., Gago, F., &amp; Fernández-Lucas, J. (2018). Characterization of an atypical, thermostable, organic solvent- and acid-tolerant 2′-deoxyribosyltransferase from Chroococcidiopsis thermalis. Applied Microbiology and Biotechnology, 102(16), 6947-6957. https://doi.org/10.1007/S00253-018-9134-Y</mods:identifier>
   <mods:identifier type="issn">0175-7598</mods:identifier>
   <mods:identifier type="doi">10.1007/s00253-018-9134-y</mods:identifier>
   <mods:identifier type="uri">https://hdl.handle.net/20.500.14352/109960</mods:identifier>
   <mods:identifier type="essn">1432-0614</mods:identifier>
   <mods:identifier type="officialurl">https://doi.org/10.1007/s00253-018-9134-y</mods:identifier>
   <mods:identifier type="relatedurl">https://link.springer.com/article/10.1007/s00253-018-9134-y</mods:identifier>
   <mods:abstract>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.</mods:abstract>
   <mods:language>
      <mods:languageTerm>eng</mods:languageTerm>
   </mods:language>
   <mods:accessCondition type="useAndReproduction">restricted access</mods:accessCondition>
   <mods:titleInfo>
      <mods:title>Characterization of an atypical, thermostable, organic solvent- and acid-tolerant 2′-deoxyribosyltransferase from Chroococcidiopsis thermalis</mods:title>
   </mods:titleInfo>
   <mods:genre>journal article</mods:genre>
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