Amino-acid racemase able to utilize a broad range of substrates. Reversibly racemizes 9 of the 19 natural chiral amino acids known, including both positively charged amino acids (Lys, Arg and His) and non-beta-branched aliphatic amino acids (Ala, Leu, Met, Ser, Gln and Asn). Among these amino acids, activity is the highest with lysine and arginine, and poor or very poor with the others (PubMed:23995642). Plays a primary role in the catabolism of basic amino acid, that allows P.putida strain KT2440 to grow on L-Lys and L-Arg as the sole source of carbon and nitrogen, through conversion to their respective D-enantiomers (PubMed:30008699). an L-alpha-amino acid = a D-alpha-amino acid L-lysine = D-lysine L-arginine = D-arginine L-glutamine = D-glutamine kcat is 274.5 sec(-1) with D-lysine as substrate. kcat is 1681.7 sec(-1) with L-lysine as substrate. kcat is 8.83 sec(-1) with D-alanine as substrate. kcat is 7.33 sec(-1) with L-alanine as substrate. Thus, the catalytic efficiency with lysine is nearly 3 orders of magnitude greater than that with alanine in both reaction directions. Cells lacking this gene exhibit a limited capacity for catabolism of L-Lys and L-Arg as the sole source of carbon and nitrogen. They don't secrete D-Lys in the growth medium. The stationary phase peptidoglycan structure does not differ between wild-type and the deletion mutant strains, indicating that products resulting from this enzyme activity are not incorporated into peptidoglycan under these conditions. Belongs to the alanine racemase family. Bsr subfamily.