<rdf:RDF xmlns:rdf="http://www.openarchives.org/OAI/2.0/rdf/" xmlns:ow="http://www.ontoweb.org/ontology/1#" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:ds="http://dspace.org/ds/elements/1.1/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/rdf/ http://www.openarchives.org/OAI/2.0/rdf.xsd">
   <ow:Publication rdf:about="oai:digibug.ugr.es:10481/73583">
      <dc:title>A New L-Proline Amide Hydrolase with Potential Application within the Amidase Process</dc:title>
      <dc:creator>Martínez Rodríguez, Sergio</dc:creator>
      <dc:creator>Contreras Montoya, Rafael</dc:creator>
      <dc:creator>Torres De Pinedo, Jesús Manuel</dc:creator>
      <dc:creator>Álvarez Cienfuegos Rodríguez, Luis</dc:creator>
      <dc:creator>Gavira Gallardo, José Antonio</dc:creator>
      <dc:subject>Amidase</dc:subject>
      <dc:subject>Amino acid</dc:subject>
      <dc:subject>Amidase process</dc:subject>
      <dc:subject>Proline</dc:subject>
      <dc:subject>Aminopeptidase</dc:subject>
      <dc:subject>S33 family</dc:subject>
      <dc:description>This research was supported by the Spanish Ministry of Science and Innovation/FEDER funds grant PID2020-116261GB-I00/AEI/10.13039/501100011033 (JAG), from the FEDER/Junta de Andalucia-Consejeria de Transformacion Economica, Industria, Conocimiento y Universidades grants P18-FR-3533 (LAC) and P12-FQM-790 (RCM), and from the University of Granada grant PPJI2017-1 (SMR).</dc:description>
      <dc:description>L-proline amide hydrolase (PAH, EC 3.5.1.101) is a barely described enzyme belonging to the peptidase S33 family, and is highly similar to prolyl aminopeptidases (PAP, EC. 3.4.11.5). Besides being an S-stereoselective character towards piperidine-based carboxamides, this enzyme also hydrolyses different L-amino acid amides, turning it into a potential biocatalyst within the Amidase Process. In this work, we report the characterization of L-proline amide hydrolase from Pseudomonas syringae (PsyPAH) together with the first X-ray structure for this class of L-amino acid amidases. Recombinant PsyPAH showed optimal conditions at pH 7.0 and 35 degrees C, with an apparent thermal melting temperature of 46 degrees C. The enzyme behaved as a monomer at the optimal pH. The L-enantioselective hydrolytic activity towards different canonical and non-canonical amino-acid amides was confirmed. Structural analysis suggests key residues in the enzymatic activity.</dc:description>
      <dc:date>2022-03-21T07:58:16Z</dc:date>
      <dc:date>2022-03-21T07:58:16Z</dc:date>
      <dc:date>2021-12-23</dc:date>
      <dc:type>info:eu-repo/semantics/article</dc:type>
      <dc:identifier>Martinez-Rodríguez, S... [et al.]. A New L-Proline Amide Hydrolase with Potential Application within the Amidase Process. Crystals 2022, 12, 18. [https://doi.org/10.3390/cryst12010018]</dc:identifier>
      <dc:identifier>http://hdl.handle.net/10481/73583</dc:identifier>
      <dc:identifier>10.3390/cryst12010018</dc:identifier>
      <dc:language>eng</dc:language>
      <dc:rights>http://creativecommons.org/licenses/by/3.0/es/</dc:rights>
      <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
      <dc:rights>Atribución 3.0 España</dc:rights>
      <dc:publisher>MDPI</dc:publisher>
   </ow:Publication>
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