N-succinylamino acid racemases: Enzymatic properties and biotechnological applications

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. •NSAR/OSBS enzymes show promiscuous N-substituted-amino acid racemase (NxAR) activity.•NSAR/OSBS enzymes are pivotal in several enzymatic cascades.•Sequence-based identification of new NSAR/OSBS enzymes is difficult; hints to overcome this problem are suggested.