The pH dependence of kinetic parameters in the amination direction of the aspartase from Hafnia alvei has been determined. The V/K for fumarate is bell shaped with pK values of 6.4 and 8.7. The maximum velocity for fumarate is also bell shaped with pK values of 7.2 and 9.1. The pH dependence of 1/K, for potassium (competitive inhibitor of ammonia) decreases at low pH with pK 7.6. Together with data [Yoon and Cook (1994) Korean J. Biochem. 27, 1-5] on the deamination direction of the aspartase, these results are consistent with two enzyme groups which are necessary for catalysis. An enzymatic group that must be deprotonated has been identified. Another enzyme group must be protonated for substrate binding. Both the general base and general acid group are in a protonation state opposite that in which they started when aspartate was bound. A proton is abstracted from C-3 of the monoanionic form of L-aspartate by an enzyme general base with, a pK of 6.3~6.6 in the absence and presence of $Mg^{2+}$ Ammonia is then expelled with the assistance of a general acid group giving $NH_{4+}$ as the product.