A New L-Proline Amide Hydrolase with Potential Application within the Amidase Process
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 <i>S</i>-stereoselective character towards piperidine-based carboxamides, this enzyme al...
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MDPI AG
2021-12-01
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| author | Sergio Martinez-Rodríguez Rafael Contreras-Montoya Jesús M. Torres Luis Álvarez de Cienfuegos Jose Antonio Gavira |
| author_facet | Sergio Martinez-Rodríguez Rafael Contreras-Montoya Jesús M. Torres Luis Álvarez de Cienfuegos Jose Antonio Gavira |
| author_sort | Sergio Martinez-Rodríguez |
| collection | DOAJ |
| 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 <i>S</i>-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 <i>Pseudomonas syringae</i> (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 °C, with an apparent thermal melting temperature of 46 °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. |
| first_indexed | 2024-03-10T01:41:03Z |
| format | Article |
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| institution | Directory Open Access Journal |
| issn | 2073-4352 |
| language | English |
| last_indexed | 2024-03-10T01:41:03Z |
| publishDate | 2021-12-01 |
| publisher | MDPI AG |
| record_format | Article |
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| spelling | doaj.art-1b994f3eba7740f5a7aa81177e2593c92023-11-23T13:23:52ZengMDPI AGCrystals2073-43522021-12-011211810.3390/cryst12010018A New L-Proline Amide Hydrolase with Potential Application within the Amidase ProcessSergio Martinez-Rodríguez0Rafael Contreras-Montoya1Jesús M. Torres2Luis Álvarez de Cienfuegos3Jose Antonio Gavira4Department of Biochemistry and Molecular Biology III and Immunology, University of Granada, 18071 Granada, Granada, SpainDepartment of Organic Chemistry, University of Granada, 18071 Granada, Granada, SpainDepartment of Biochemistry and Molecular Biology III and Immunology, University of Granada, 18071 Granada, Granada, SpainDepartment of Organic Chemistry, University of Granada, 18071 Granada, Granada, SpainLaboratory of Crystallographic Studies, Andalusian Institute of Earth Sciences, C.S.I.C. University of Granada, Avenida de las Palmeras No. 4, 18100 Armilla, Granada, SpainL-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 <i>S</i>-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 <i>Pseudomonas syringae</i> (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 °C, with an apparent thermal melting temperature of 46 °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.https://www.mdpi.com/2073-4352/12/1/18amidaseamino acidamidase processprolineaminopeptidaseS33 family |
| spellingShingle | Sergio Martinez-Rodríguez Rafael Contreras-Montoya Jesús M. Torres Luis Álvarez de Cienfuegos Jose Antonio Gavira A New L-Proline Amide Hydrolase with Potential Application within the Amidase Process Crystals amidase amino acid amidase process proline aminopeptidase S33 family |
| title | A New L-Proline Amide Hydrolase with Potential Application within the Amidase Process |
| title_full | A New L-Proline Amide Hydrolase with Potential Application within the Amidase Process |
| title_fullStr | A New L-Proline Amide Hydrolase with Potential Application within the Amidase Process |
| title_full_unstemmed | A New L-Proline Amide Hydrolase with Potential Application within the Amidase Process |
| title_short | A New L-Proline Amide Hydrolase with Potential Application within the Amidase Process |
| title_sort | new l proline amide hydrolase with potential application within the amidase process |
| topic | amidase amino acid amidase process proline aminopeptidase S33 family |
| url | https://www.mdpi.com/2073-4352/12/1/18 |
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