<?xml version="1.0" encoding="ISO-8859-1"?><article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance">
<front>
<journal-meta>
<journal-id>1405-888X</journal-id>
<journal-title><![CDATA[TIP. Revista especializada en ciencias químico-biológicas]]></journal-title>
<abbrev-journal-title><![CDATA[TIP]]></abbrev-journal-title>
<issn>1405-888X</issn>
<publisher>
<publisher-name><![CDATA[Universidad Nacional Autónoma de México, Facultad de Estudios Superiores Zaragoza]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S1405-888X2019000100209</article-id>
<article-id pub-id-type="doi">10.22201/fesz.23958723e.2019.0.191</article-id>
<title-group>
<article-title xml:lang="es"><![CDATA[Aspectos estructurales y funcionales de la N-Succinil-L, L-diaminopimelato desuccinilasa, una enzima clave para el crecimiento bacteriano y un blanco para el control antimicrobiano]]></article-title>
<article-title xml:lang="en"><![CDATA[Structural and Functional Features of a N-Succinyl-L, L-diaminopimelate desuccinylase, acritical enzyme for bacterial growth and anantimicrobial target]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Díaz-Sánchez]]></surname>
<given-names><![CDATA[Ángel Gabriel]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Terrazas-López]]></surname>
<given-names><![CDATA[Manuel]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Aguirre-Reyes]]></surname>
<given-names><![CDATA[Luis Guadalupe]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Lobo-Galo]]></surname>
<given-names><![CDATA[Naún]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Álvarez-Parrilla]]></surname>
<given-names><![CDATA[Emilio]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Martínez-Martínez]]></surname>
<given-names><![CDATA[Alejandro]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidad Autónoma de Ciudad Juárez Instituto de Ciencias Biomédicas Departamento de Ciencias Químico Biológicas]]></institution>
<addr-line><![CDATA[Ciudad Juárez Chihuahua]]></addr-line>
<country>Mexico</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>00</month>
<year>2019</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>00</month>
<year>2019</year>
</pub-date>
<volume>22</volume>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_arttext&amp;pid=S1405-888X2019000100209&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_abstract&amp;pid=S1405-888X2019000100209&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_pdf&amp;pid=S1405-888X2019000100209&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen La N-Succinil-L, L-diaminopimelato desuccinilasa (DapE) es una amidohidrolasa dependiente de iones de zinc, homodimérica estricta, que cataliza la descomposición del N-succinil-L, L-2,6-diaminopimelato (NSDAP), en succinato y diaminopimelato (DAP). Reacción que constituye la única fuente de meso-diaminopimelato (mDAP) y L-Lys en la mayoría de las bacterias. DapE es esencial para el crecimiento bacteriano y un blanco farmacológico antimicrobiano. El desarrollo de los inhibidores anti-DapE debe tener en cuenta las propiedades dinámicas de la enzima. Se buscan compuestos que interfieran con la formación del agujero del oxianión, en donde participan grupos de ambas subunidades del dímero, que se acomoda en posición catalítica mediante el cambio conformacional de la enzima de un estado abierto a uno cerrado, después de la unión del sustrato; estabilizando a los intermediarios de reacción y produciendo un descenso en la energía de activación. Con base en el análisis cristalográfico y el acoplamiento del sustrato en DapE que se presenta en este trabajo, se discute el papel de la flexibilidad conformacional de la enzima en la hidrólisis del sustrato. Se observa que tanto el grupo carbonilo del sustrato es susceptible al ataque como una molécula de agua ubicada en el sitio activo y se encuentran cercanos a la trayectoria de ataque, en el ángulo de Bürgi-Dunitz.]]></p></abstract>
<abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract N-Succinyl-L, L-diaminopimelate desuccinylase (DapE) is a strictly dimeric zinc-dependent amidohydrolase, which catalyzes the decomposition of N-succinyl-L, L-2,6-diaminopimelate (NSDAP), into succinate and diaminopimelate (DAP). This reaction constitutes the only source of meso-diaminopimelate (mDAP) and L-Lys in most bacteria. DapE is essential for bacterial growth and a pharmacological antimicrobial target. The development of anti-DapE inhibitors must take into account the dynamic properties of the enzyme. There is a special interest in compounds that block the formation of the oxyanion hole, where is assembled with groups of both subunits of the dimer and accommodated in its catalytic position by the conformational change of the enzyme from an open to a closed state, upon productive substrate binding. The hole stabilizes reaction intermediaries, thus contributing to the decrease in the activation energy. Based on the crystallographic analysis and the coupling of the substrate into DapE presented in this work, the role of the conformational flexibility of the enzyme in substrate hydrolysis is discussed. It is observed that the susceptible carbonyl group of the substrate and a water molecule located in the active site are near to the trajectory of attack, the Bürgi-Dunitz angle.]]></p></abstract>
<kwd-group>
<kwd lng="es"><![CDATA[estructura de proteínas]]></kwd>
<kwd lng="es"><![CDATA[función de proteínas]]></kwd>
<kwd lng="es"><![CDATA[enzimas]]></kwd>
<kwd lng="es"><![CDATA[inhibición]]></kwd>
<kwd lng="es"><![CDATA[dinámica conformacional]]></kwd>
<kwd lng="en"><![CDATA[protein structure]]></kwd>
<kwd lng="en"><![CDATA[protein function]]></kwd>
<kwd lng="en"><![CDATA[enzymes]]></kwd>
<kwd lng="en"><![CDATA[inhibition]]></kwd>
<kwd lng="en"><![CDATA[conformational dynamics]]></kwd>
</kwd-group>
</article-meta>
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