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A New L-Proline Amide Hydrolase with Potential Application within the Amidase Process
dc.contributor.author | Martínez Rodríguez, Sergio | |
dc.contributor.author | Contreras Montoya, Rafael | |
dc.contributor.author | Torres De Pinedo, Jesús Manuel | |
dc.contributor.author | Álvarez Cienfuegos Rodríguez, Luis | |
dc.contributor.author | Gavira Gallardo, José Antonio | |
dc.date.accessioned | 2022-03-21T07:58:16Z | |
dc.date.available | 2022-03-21T07:58:16Z | |
dc.date.issued | 2021-12-23 | |
dc.identifier.citation | 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] | es_ES |
dc.identifier.uri | http://hdl.handle.net/10481/73583 | |
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). | es_ES |
dc.description.abstract | 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. | es_ES |
dc.description.sponsorship | Spanish Government | es_ES |
dc.description.sponsorship | European Commission PID2020-116261GB-I00/AEI/10.13039/501100011033 | es_ES |
dc.description.sponsorship | FEDER/Junta de Andalucia-Consejeria de Transformacion Economica, Industria, Conocimiento y Universidades P18-FR-3533 P12-FQM-790 | es_ES |
dc.description.sponsorship | University of Granada PPJI2017-1 CTS-202 | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | MDPI | es_ES |
dc.rights | Atribución 3.0 España | * |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es/ | * |
dc.subject | Amidase | es_ES |
dc.subject | Amino acid | es_ES |
dc.subject | Amidase process | es_ES |
dc.subject | Proline | es_ES |
dc.subject | Aminopeptidase | es_ES |
dc.subject | S33 family | es_ES |
dc.title | A New L-Proline Amide Hydrolase with Potential Application within the Amidase Process | es_ES |
dc.type | journal article | es_ES |
dc.rights.accessRights | open access | es_ES |
dc.identifier.doi | 10.3390/cryst12010018 | |
dc.type.hasVersion | VoR | es_ES |