N-succinylamino acid racemase (NSAR)

N-succinylamino acid racemase (NSAR) is an enzyme that catalyzes the racemization (conversion between L- and D- forms) of N-succinylated amino acids, a reaction important in the biosynthetic pathways that generate enantiopure amino acids for industrial use[2][3][4][6]. The enzyme acts on a broad range of N-acylated amino acids, such as N-succinyl-phenylglycine and N-succinyl-methionine, and is a member of the enolase superfamily, requiring a divalent metal ion (like Co²⁺ or Mg²⁺) for full activity[2][5][6]. Structurally, NSAR is typically a multimeric enzyme (often tetrameric or octameric) with a high degree of thermostability in certain bacterial species[5]. The enzyme has significant biotechnological relevance for the industrial production of chiral amino acids used as building blocks for drugs and biochemical synthesis, though it is not a recognized drug or disease target in clinical medicine[3][4][5]. Some NSARs exhibit dual activity with o-succinylbenzoate synthase (OSBS), illustrating functional diversity within this enzyme family[1][3].

Other names

N-acylamino acid racemaseN-acetyl-amino acid racemaseNSAARNAAARNxAR

Catalyzes the racemization of N-succinylamino acids through a two-base mechanism involving key lysine residues and a divalent metal ion (isomerization of amino acid enantiomers)