@misc{10481/73583,
year = {2021},
month = {12},
url = {http://hdl.handle.net/10481/73583},
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.},
organization = {Spanish Government},
organization = {European Commission	PID2020-116261GB-I00/AEI/10.13039/501100011033},
organization = {FEDER/Junta de Andalucia-Consejeria de Transformacion Economica, Industria, Conocimiento y Universidades	P18-FR-3533	
P12-FQM-790},
organization = {University of Granada	PPJI2017-1	
CTS-202},
publisher = {MDPI},
keywords = {Amidase},
keywords = {Amino acid},
keywords = {Amidase process},
keywords = {Proline},
keywords = {Aminopeptidase},
keywords = {S33 family},
title = {A New L-Proline Amide Hydrolase with Potential Application within the Amidase Process},
doi = {10.3390/cryst12010018},
author = {Martínez Rodríguez, Sergio and Contreras Montoya, Rafael and Torres De Pinedo, Jesús Manuel and Álvarez Cienfuegos Rodríguez, Luis and Gavira Gallardo, José Antonio},
}