Amino acid racemase that shows relatively high activity toward leucine, which is the preferred substrate, and methionine (PubMed:33468590). Also exhibits lower levels of activity toward phenylalanine and alanine, and trace activities toward isoleucine and valine (PubMed:33468590). L-leucine = D-leucine L-methionine = D-methionine Activity is completely abolished in the presence of hydroxylamine, a known specific pyridoxal-phosphate inhibitor. kcat is 108 sec(-1) with D-leucine as substrate. kcat is 43.3 sec(-1) with L-leucine as substrate. kcat is 86.0 sec(-1) with D-methionine as substrate. kcat is 54.4 sec(-1) with L-methionine as substrate. Optimum pH is 5.0 for leucine racemase activity. Optimum temperature is 70 degrees Celsius for D-leucine to L-leucine reaction. Optimum temperature is 75 degrees Celsius for L-leucine to D-leucine reaction. Homotetramer. The disruption mutant displays growth in medium with L-leucine but cannot grow with D-leucine. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.