N-succinylamino acid racemases: Enzymatic properties and biotechnological applications |
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Affiliation: | 1. Departamento de Bioquímica y Biología Molecular III e Inmunología, Universidad de Granada, Facultad de Medicina, Granada 18071, Spain;2. Laboratorio de Estudios Cristalográficos, CSIC, 18100 Granada, Spain;3. Centro Nacional de Investigaciones Oncológicas, Madrid, Spain;1. Istituto di Biostrutture e Bioimmagini, C.N.R., Via Mezzocannone 16, I-80134 Napoli, Italy;2. Departamento de Bioquímica y Biología Molecular, Facultad de Química, Universidad Complutense, E-28040 Madrid, Spain;3. Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania ‘Luigi Vanvitelli’, Via Vivaldi 43, I-81100 Caserta, Italy |
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Abstract: | The N-succinylamino acid racemase/o-succinylbenzoate synthase (NSAR/OSBS) subfamily from the enolase superfamily contains different enzymes showing promiscuous N-substituted-amino acid racemase (NxAR) activity. These enzymes were originally named as N-acylamino acid racemases because of their industrial application. Nonetheless, they are pivotal in several enzymatic cascades due to their versatility to catalyze a wide substrate spectrum, allowing the production of optically pure d- or l-amino acids from cheap precursors. These compounds are of paramount economic interest, since they are used as food additives, in the pharmaceutical and cosmetics industries and/or as chiral synthons in organic synthesis. Despite its economic importance, the discovery of new N-succinylamino acid racemases has become elusive, since classical sequence-based annotation methods proved ineffective in their identification, due to a high sequence similarity among the members of the enolase superfamily. During the last decade, deeper investigations into different members of the NSAR/OSBS subfamily have shed light on the classification and identification of NSAR enzymes with NxAR activity of biotechnological potential. This review aims to gather the dispersed information on NSAR/OSBS members showing NxAR activity over recent decades, focusing on their biotechnological applications and providing practical advice to identify new enzymes. |
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