N-succinylamino acid racemases: Enzymatic properties and biotechnological applications.
Biochim Biophys Acta Proteins Proteom
; 1868(4): 140377, 2020 04.
Article
em En
| MEDLINE
| ID: mdl-31982578
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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1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Biotecnologia
/
Isomerases de Aminoácido
Idioma:
En
Revista:
Biochim Biophys Acta Proteins Proteom
Ano de publicação:
2020
Tipo de documento:
Article