Partial purification and characterization of an enzyme involved in the formation of beta-aspartyl dipeptides in rat kidney.

The formation of beta-aspartyl-glycine from asparagine and glycine was demonstrated in the supernatant of rat kidney. The enzyme involved in this process was partially purified. Based on the properties of the enzyme reaction and the coincidence of purification rates of this activity and asparaginase, it can be speculated that the enzyme is a kind of asparaginase. Examination of the preference for beta-aspartyl donors and acceptors showed that asparagine and glycine were the preferred donor and acceptor, respectively. beta-Aspartyl dipeptides also transferred their aspartyl residues to amino acids. Amino acids other than glycine also accepted the aspartyl moiety from the donors.