Acts as a N-succinylamino acid racemase (NSAR) that catalyzes the racemization of N-succinyl-L-phenylglycine and N-succinyl-D/L-phenylalanine (PubMed:24872444, PubMed:25875730). Can catalyze the racemization of a broad range of N-acylamino acids, including N-acetyl-D/L-methionine, N-acetyl-D/L-phenylalanine, N-acetyl-L-glutamine, N-acetyl-L-tryptophan, N-acetyl-L-leucine, N-formyl-D-methionine, N-formyl-D-norleucine, N-carbamoyl-D-methionine and N-carbamoyl-D-norleucine (PubMed:15313614, PubMed:16650857, PubMed:25875730). Also converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (PubMed:24872444). Catalyzes both N-succinylamino acid racemization and OSB synthesis at equivalent rates (PubMed:24872444). However, NSAR activity is probably the protein's biological function, because menaquinone biosynthesis genes are missing in this species (Probable). N(alpha)-acetyl-D-methionine = N(alpha)-acetyl-L-methionine N-acetyl-D-phenylalanine = N-acetyl-L-phenylalanine N-acetyl-L-glutamine = N-acetyl-D-glutamine N-acetyl-L-tryptophan = N-acetyl-D-tryptophan N-acetyl-L-leucine = N-acetyl-D-leucine (1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H2O Binds 1 divalent metal cation per subunit. Inhibited by salicyl hydroxamate, an inhibitor of o-succinylbenzoate synthase. kcat is 520 sec(-1) with N-succinyl-L-phenylglycine as substrate (PubMed:24872444). kcat is 8.5 min(-1) with N-acetyl-D-methionine as substrate (PubMed:15313614). kcat is 9.9 min(-1) with N-acetyl-L-methionine as substrate (PubMed:15313614). kcat is 6.85 min(-1) with N-acetyl-L-methionine as substrate (PubMed:16650857). kcat is 8.1 sec(-1) with SHCHC as substrate (PubMed:24872444). Optimum pH is 8.0. Optimum temperature is 60 degrees Celsius. Stable at 55 degrees Celsius. Retains 80% of activity at 70 degrees Celsius. Homooctamer. Can be used in concert with an aminoacylase to produce enantiopure alpha-amino acids, a process that has potential industrial applications (PubMed:15313614). Introduction of inter-subunit S-S bridges is a feasible and robust approach to increase the thermostability of the enzyme without losing catalytic efficiency as long as the active-site remains viable (PubMed:16650857). Belongs to the mandelate racemase/muconate lactonizing enzyme family. MenC type 2 subfamily.