<?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>2026-06-29T02:43:52Z</responseDate><request verb="GetRecord" identifier="oai:docta.ucm.es:20.500.14352/103372" metadataPrefix="qdc">https://docta.ucm.es/rest/oai/request</request><GetRecord><record><header><identifier>oai:docta.ucm.es:20.500.14352/103372</identifier><datestamp>2025-03-18T12:51:27Z</datestamp><setSpec>com_20.500.14352_14</setSpec><setSpec>col_20.500.14352_15</setSpec></header><metadata><qdc:qualifieddc xmlns:qdc="http://dspace.org/qualifieddc/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://purl.org/dc/elements/1.1/ http://dublincore.org/schemas/xmls/qdc/2006/01/06/dc.xsd http://purl.org/dc/terms/ http://dublincore.org/schemas/xmls/qdc/2006/01/06/dcterms.xsd http://dspace.org/qualifieddc/ http://www.ukoln.ac.uk/metadata/dcmi/xmlschema/qualifieddc.xsd">
   <dc:title>The cytotoxin α‐sarcin behaves as a cyclizing ribonuclease</dc:title>
   <dc:creator>Lacadena García-Gallo, Francisco Javier</dc:creator>
   <dc:creator>Martínez Del Pozo, Álvaro</dc:creator>
   <dc:creator>Valle Lacadena</dc:creator>
   <dc:creator>Martínez Ruiz, Antonio</dc:creator>
   <dc:creator>Mancheño Gómez, José Miguel</dc:creator>
   <dc:creator>Oñaderra Sánchez, Mercedes</dc:creator>
   <dc:creator>Gavilanes Franco, José Gregorio</dc:creator>
   <dcterms:abstract>The hydrolysis of adenylyl(3PC5P)adenosine (ApA)
and guanylyl(3PC5P)adenosine (GpA) dinucleotides by the
cytotoxic protein K-sarcin has been studied. Quantitative
analysis of the reaction has been performed through reversephase chromatographic (HPLC) separation of the resulting
products. The hydrolysis of the 3P-5P phosphodiester bond of
these substrates yields the 2P-3P cyclic mononucleotide; this
intermediate is converted into the corresponding 3P-monophosphate derivative as the final product of the reaction. The
values of the apparent Michaelis constant (KM), kcat and kcat/
KM have also been calculated. The obtained results fit into a twostep mechanism for the enzymatic activity of K-sarcin and allow
to consider this protein as a cyclizing RNase.
z 1998 Federation of European Biochemical Societies.</dcterms:abstract>
   <dcterms:dateAccepted>2024-04-23T11:00:03Z</dcterms:dateAccepted>
   <dcterms:available>2024-04-23T11:00:03Z</dcterms:available>
   <dcterms:created>2024-04-23T11:00:03Z</dcterms:created>
   <dcterms:issued>1998-03-06</dcterms:issued>
   <dc:type>journal article</dc:type>
   <dc:identifier>https://hdl.handle.net/20.500.14352/103372</dc:identifier>
   <dc:identifier>0014-5793</dc:identifier>
   <dc:identifier>1873-3468</dc:identifier>
   <dc:identifier>10.1016/s0014-5793(98)00137-9</dc:identifier>
   <dc:language>eng</dc:language>
   <dc:relation>Lacadena Javier, Martı́nez del Pozo Alvaro, Lacadena Valle, Martı́nez-Ruiz Antonio, Mancheño José M, Oñaderra Mercedes and Gavilanes José G(1998), The cytotoxin α-sarcin behaves as a cyclizing ribonuclease, FEBS Letters, 424, doi: 10.1016/S0014-5793(98)00137-9</dc:relation>
   <dc:rights>open access</dc:rights>
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