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dc.contributor.authorMartínez Rodríguez, Sergio 
dc.contributor.authorContreras Montoya, Rafael
dc.contributor.authorTorres De Pinedo, Jesús Manuel 
dc.contributor.authorÁlvarez Cienfuegos Rodríguez, Luis 
dc.contributor.authorGavira Gallardo, José Antonio 
dc.date.accessioned2022-03-21T07:58:16Z
dc.date.available2022-03-21T07:58:16Z
dc.date.issued2021-12-23
dc.identifier.citationMartinez-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]es_ES
dc.identifier.urihttp://hdl.handle.net/10481/73583
dc.descriptionThis 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).es_ES
dc.description.abstractL-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.es_ES
dc.description.sponsorshipSpanish Governmentes_ES
dc.description.sponsorshipEuropean Commission PID2020-116261GB-I00/AEI/10.13039/501100011033es_ES
dc.description.sponsorshipFEDER/Junta de Andalucia-Consejeria de Transformacion Economica, Industria, Conocimiento y Universidades P18-FR-3533 P12-FQM-790es_ES
dc.description.sponsorshipUniversity of Granada PPJI2017-1 CTS-202es_ES
dc.language.isoenges_ES
dc.publisherMDPIes_ES
dc.rightsAtribución 3.0 España*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/es/*
dc.subjectAmidasees_ES
dc.subjectAmino acid es_ES
dc.subjectAmidase processes_ES
dc.subjectProlinees_ES
dc.subjectAminopeptidasees_ES
dc.subjectS33 familyes_ES
dc.titleA New L-Proline Amide Hydrolase with Potential Application within the Amidase Processes_ES
dc.typejournal articlees_ES
dc.rights.accessRightsopen accesses_ES
dc.identifier.doi10.3390/cryst12010018
dc.type.hasVersionVoRes_ES


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Atribución 3.0 España
Except where otherwise noted, this item's license is described as Atribución 3.0 España